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Human Metabolome Database Version 2.5

 

Showing metabocard for Glutathione (HMDB00125)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-11-24 20:56:01
Accession Number HMDB00125
Secondary Accession Numbers HMDB01463; HMDB06960
Common Name Glutathione
Description Glutathione is a compound synthesized from cysteine, perhaps the most important member of the body's toxic waste disposal team. Like cysteine, glutathione contains the crucial thiol (-SH) group that makes it an effective antioxidant. There are virtually no living organisms on this planet-animal or plant whose cells don't contain some glutathione. Scientists have speculated that glutathione was essential to the very development of life on earth. glutathione has many roles; in none does it act alone. It is a coenzyme in various enzymatic reactions. The most important of these are redox reactions, in which the thiol grouping on the cysteine portion of cell membranes protects against peroxidation; and conjugation reactions, in which glutathione (especially in the liver) binds with toxic chemicals in order to detoxify them. glutathione is also important in red and white blood cell formation and throughout the immune system. glutathione's clinical uses include the prevention of oxygen toxicity in hyperbaric oxygen therapy, treatment of lead and other heavy metal poisoning, lowering of the toxicity of chemotherapy and radiation in cancer treatments, and reversal of cataracts. (http://www.dcnutrition.com/AminoAcids/) glutathione participates in leukotriene synthesis and is a cofactor for the enzyme glutathione peroxidase. It is also important as a hydrophilic molecule that is added to lipophilic toxins and waste in the liver during biotransformation before they can become part of the bile. glutathione is also needed for the detoxification of methylglyoxal, a toxin produced as a by-product of metabolism. This detoxification reaction is carried out by the glyoxalase system. Glyoxalase I (EC 4.4.1.5) catalyzes the conversion of methylglyoxal and reduced glutathione to S-D-Lactoyl-glutathione. Glyoxalase II (EC 3.1.2.6) catalyzes the hydrolysis of S-D-Lactoyl-glutathione to glutathione and D-lactate. GSH is known as a substrate in both conjugation reactions and reduction reactions, catalyzed by glutathione S-transferase enzymes in cytosol, microsomes, and mitochondria. However, it is also capable of participating in non-enzymatic conjugation with some chemicals, as in the case of n-acetyl-p-benzoquinone imine (NAPQI), the reactive cytochrome P450-reactive metabolite formed by acetaminophen, that becomes toxic when GSH is depleted by an overdose (of acetaminophen). glutathione in this capacity binds to NAPQI as a suicide substrate and in the process detoxifies it, taking the place of cellular protein thiol groups which would otherwise be covalently modified; when all GSH has been spent, NAPQI begins to react with the cellular proteins, killing the cells in the process. The preferred treatment for an overdose of this painkiller is the administration (usually in atomized form) of N-acetylcysteine, which is used by cells to replace spent GSSG and renew the usable GSH pool. (http://en.wikipedia.org/wiki/glutathione)
Synonyms
  1. 5-L-Glutamyl-L-cysteinylglycine
  2. Agifutol S
  3. Bakezyme RX
  4. Copren
  5. Deltathione
  6. GSH
  7. Glutathion
  8. Glutathione
  9. Glutathione red
  10. Glutathione reduced
  11. Glutathione-SH
  12. Glutatiol
  13. Glutatione
  14. Glutide
  15. Glutinal
  16. L-g-glutamyl-L-cysteinyl-glycine
  17. L-gamma-glutamyl-L-cysteinyl-glycine
  18. Isethion
  19. L-Glutathione
  20. L-Glutathione reduce
  21. L-gamma-glutamyl-L-cysteinylglycine
  22. L-glutamyl-L-cysteinylglycine
  23. Ledac
  24. Neuthion
  25. Reduced glutathione
  26. Tathion
  27. Tathione
  28. Triptide
  29. gamma-Glutamylcysteinylglycine
  30. gamma-L-Glutamyl-L-cysteinylglycine
  31. gamma-L-glutamyl-L-cysteinyl-glycine
  32. red. glutathione
Chemical IUPAC Name (2S)-2-amino-4-[[(1R)-1-(carboxymethylcarbamoyl)-2-sulfanyl-ethyl]carbamoyl]butanoic acid
Chemical Formula C10H17N3O6S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Polypeptides
Sub Class
  • Tripeptides
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • thiol (sulfanyl compound)
  • alkylthiol
  • alpha-aminoacid
Biofunction
  • Component of Glutamate metabolism
  • Component of Glutathione metabolism
Application
Source
  • Endogenous
Average Molecular Weight 307.323
Monoisotopic Molecular Weight 307.083801
Isomeric SMILES N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O)C(O)=O
Canonical SMILES NC(CCC(=O)NC(CS)C(=O)NCC(O)=O)C(O)=O
KEGG Compound ID C00051 Link Image
BioCyc ID OXIDIZED-GLUTATHIONE Link Image
BiGG ID 33669 Link Image
Wikipedia Link Glutathione Link Image
NuGOwiki Link HMDB00125 Link Image
Metagene Link HMDB00125 Link Image
METLIN ID 44 Link Image
PubChem Compound 124886 Link Image
PubChem Substance 821009 Link Image
ChEBI ID 16856 Link Image
CAS Registry Number 70-18-8
InChI Identifier InChI=1/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) 195 oC
Experimental Water Solubility 292.5 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 1000.0 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 0.879 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.74 [Predicted by ALOGPS]; -6.4 [Predicted by PubChem via XLOGP]; -5.41 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 11GS Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • endoplasmic reticulum
  • Extracellular
  • mitochondria
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues
Concentrations (Normal)
Biofluid Blood
Value 37.03 +/- 4.76 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments In plasma, n=15, healthy volunteers, age of volunteers: 27-50 years (mean of 42.3 +/- 18.6 years)
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid Blood
Value 12.5 +/- 5.2 uM
Age Infant:0-1 yr old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 10.9 +/- 4.5 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 12.00 +/- 3.00 uM
Age Adolescent:13-18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 12.8 +/- 4.6 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Pastore A, Massoud R, Motti C, Lo Russo A, Fucci G, Cortese C, Federici G: Fully automated assay for total homocysteine, cysteine, cysteinylglycine, glutathione, cysteamine, and 2-mercaptopropionylglycine in plasma and urine. Clin Chem. 1998 Apr;44(4):825-32. [PubMed Link Image]
Biofluid Blood
Value 4.35 +/- 2.10 uM
Age Adolescent:13-18 yrs old
Sex Male
Patient information Normal
Comments Total serum glutathione in adolescent male offspring of parents without premature Coronary Heart Disease (CHD)
References
  • Morrison JA, Jacobsen DW, Sprecher DL, Robinson K, Khoury P, Daniels SR: Serum glutathione in adolescent males predicts parental coronary heart disease. Circulation. 1999 Nov 30;100(22):2244-7. [PubMed Link Image]
Biofluid Blood
Value 3.20 +/- 2.20 uM
Age Adolescent:13-18 yrs old
Sex Male
Patient information Normal
Comments Total serum glutathione in adolescent male offspring of parents with premature Coronary Heart Disease (CHD)
References
  • Morrison JA, Jacobsen DW, Sprecher DL, Robinson K, Khoury P, Daniels SR: Serum glutathione in adolescent males predicts parental coronary heart disease. Circulation. 1999 Nov 30;100(22):2244-7. [PubMed Link Image]
Biofluid Cellular Cytoplasm
Value 3210 (1710-4710) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Biofluid CSF
Value 1.2 +/- 0.16 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
Biofluid Urine
Value 0.065 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Iida M, Yasuhara T, Mochizuki H, Takakura H, Yanagisawa T, Kubo H: Two Japanese brothers with hereditary gamma-glutamyl transpeptidase deficiency. J Inherit Metab Dis. 2005;28(1):49-55. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 30.22 +/- 2.55 uM
Age Children:1-13 yrs old
Sex N/A
Condition Canavan disease
Comments n=10, mean age 4.6 +/- 2.3 years, reduced glutathione
References
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Biofluid CSF
Value 0.19 +/- 0.05 uM
Age Children:1-13 yrs old
Sex N/A
Condition Traumatic brain injury
Comments Traumatic brain injury in children
References
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
Biofluid CSF
Value 4.56 +/- 0.7 uM
Age Adult:>18 yrs old
Sex N/A
Condition Multiple sclerosis
Comments Under treatment with Acetyl-L-carnitine
References
  • Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [PubMed Link Image]
Biofluid CSF
Value 2.58 +/- 1.2 uM
Age Adult:>18 yrs old
Sex N/A
Condition Multiple sclerosis
Comments Not Available
References
  • Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [PubMed Link Image]
Associated Disorders
Condition References
Canavan disease
  • Tavazzi B, Lazzarino G, Leone P, Amorini AM, Bellia F, Janson CG, Di Pietro V, Ceccarelli L, Donzelli S, Francis JS, Giardina B: Simultaneous high performance liquid chromatographic separation of purines, pyrimidines, N-acetylated amino acids, and dicarboxylic acids for the chemical diagnosis of inborn errors of metabolism. Clin Biochem. 2005 Nov;38(11):997-1008. Epub 2005 Sep 1. [PubMed Link Image]
Multiple sclerosis
  • Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [PubMed Link Image]
Traumatic brain injury
  • Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Glutathione Metabolism SMP00015 Link Image map00480 Link Image
Pyruvaldehyde Degradation SMP00459 Link Image
General References
  1. Djurhuus R, Segadal K, Svardal AM: Glutathione in blood cells decreases without DNA breaks after a simulated saturation dive to 250 msw. Aviat Space Environ Med. 2006 Jun;77(6):597-604. [PubMed Link Image]
  2. Bayir H, Kagan VE, Tyurina YY, Tyurin V, Ruppel RA, Adelson PD, Graham SH, Janesko K, Clark RS, Kochanek PM: Assessment of antioxidant reserves and oxidative stress in cerebrospinal fluid after severe traumatic brain injury in infants and children. Pediatr Res. 2002 May;51(5):571-8. [PubMed Link Image]
  3. Hung CR: Effect of lysozyme chloride on betel quid chewing aggravated gastric oxidative stress and hemorrhagic ulcer in diabetic rats. World J Gastroenterol. 2005 Oct 7;11(37):5853-8. [PubMed Link Image]
  4. Grattagliano I, Portincasa P, Palmieri VO, Palasciano G: Contribution of canalicular glutathione efflux to bile formation. From cholestasis associated alterations to pharmacological intervention to modify bile flow. Curr Drug Targets Immune Endocr Metabol Disord. 2005 Jun;5(2):153-61. [PubMed Link Image]
  5. Calvo-Marzal P, Chumbimuni-Torres KY, Hoehr NF, Kubota LT: Determination of glutathione in hemolysed erythrocyte with amperometric sensor based on TTF-TCNQ. Clin Chim Acta. 2006 Sep;371(1-2):152-8. Epub 2006 May 2. [PubMed Link Image]
  6. Calabrese V, Scapagnini G, Ravagna A, Bella R, Butterfield DA, Calvani M, Pennisi G, Giuffrida Stella AM: Disruption of thiol homeostasis and nitrosative stress in the cerebrospinal fluid of patients with active multiple sclerosis: evidence for a protective role of acetylcarnitine. Neurochem Res. 2003 Sep;28(9):1321-8. [PubMed Link Image]
  7. Sohlenius-Sternbeck AK, Schmidt S: Impaired glutathione-conjugating capacity by cryopreserved human and rat hepatocytes. Xenobiotica. 2005 Jul;35(7):727-36. [PubMed Link Image]
  8. Iida M, Yasuhara T, Mochizuki H, Takakura H, Yanagisawa T, Kubo H: Two Japanese brothers with hereditary gamma-glutamyl transpeptidase deficiency. J Inherit Metab Dis. 2005;28(1):49-55. [PubMed Link Image]
  9. Briz O, Romero MR, Martinez-Becerra P, Macias RI, Perez MJ, Jimenez F, San Martin FG, Marin JJ: OATP8/1B3-mediated cotransport of bile acids and glutathione: an export pathway for organic anions from hepatocytes? J Biol Chem. 2006 Oct 13;281(41):30326-35. Epub 2006 Jul 28. [PubMed Link Image]
  10. Czeczot H, Scibior D, Skrzycki M, Podsiad M: [Antioxidant barrier in patients with gastric cancer--preliminary study] Pol Merkur Lekarski. 2005 Oct;19(112):521-5. [PubMed Link Image]
  11. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  12. Czeczot H, Scibior D, Skrzycki M, Podsiad M: Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma. Acta Biochim Pol. 2006;53(1):237-42. Epub 2006 Jan 9. [PubMed Link Image]
  13. Kawakami Y, Monobe M, Kuwabara K, Fujita T, Maeda M, Fujino O, Kojima S, Fukunaga Y: A comparative study of nitric oxide, glutathione, and glutathione peroxidase activities in cerebrospinal fluid from children with convulsive diseases/children with aseptic meningitis. Brain Dev. 2006 May;28(4):243-6. Epub 2006 Jan 10. [PubMed Link Image]
  14. Kaynar H, Meral M, Turhan H, Keles M, Celik G, Akcay F: Glutathione peroxidase, glutathione-S-transferase, catalase, xanthine oxidase, Cu-Zn superoxide dismutase activities, total glutathione, nitric oxide, and malondialdehyde levels in erythrocytes of patients with small cell and non-small cell lung cancer. Cancer Lett. 2005 Sep 28;227(2):133-9. Epub 2005 Jan 8. [PubMed Link Image]
  15. Tsai CC, Chen HS, Chen SL, Ho YP, Ho KY, Wu YM, Hung CC: Lipid peroxidation: a possible role in the induction and progression of chronic periodontitis. J Periodontal Res. 2005 Oct;40(5):378-84. [PubMed Link Image]
  16. Wielandt AM, Vollrath V, Farias M, Chianale J: Bucillamine induces glutathione biosynthesis via activation of the transcription factor Nrf2. Biochem Pharmacol. 2006 Aug 14;72(4):455-62. Epub 2006 Jun 27. [PubMed Link Image]
  17. Oztezcan S, Balkan J, Dogru-Abbasoglu S, Cevikbas U, Aykac-Toker G, Uysal M: Resistance of erythrocytes to lipid peroxidation in cirrhotic rats. Arch Med Res. 2005 Sep-Oct;36(5):459-63. [PubMed Link Image]
  18. Schulpis KH, Papassotiriou I, Parthimos T, Tsakiris T, Tsakiris S: The effect of L-cysteine and glutathione on inhibition of Na+, K+-ATPase activity by aspartame metabolites in human erythrocyte membrane. Eur J Clin Nutr. 2006 May;60(5):593-7. [PubMed Link Image]
  19. Zamek-Gliszczynski MJ, Hoffmaster KA, Nezasa K, Tallman MN, Brouwer KL: Integration of hepatic drug transporters and phase II metabolizing enzymes: mechanisms of hepatic excretion of sulfate, glucuronide, and glutathione metabolites. Eur J Pharm Sci. 2006 Apr;27(5):447-86. Epub 2006 Feb 10. [PubMed Link Image]
  20. Iwasaki Y, Hoshi M, Ito R, Saito K, Nakazawa H: Analysis of glutathione and glutathione disulfide in human saliva using hydrophilic interaction chromatography with mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. 2006 Jul 24;839(1-2):74-9. Epub 2006 Apr 18. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Prostaglandin E synthase
  2. Glutathione reductase, mitochondrial precursor
  3. Lactoylglutathione lyase
  4. Gamma-glutamyltranspeptidase 1 precursor
  5. Glutathione synthetase
  6. Leukotriene C4 synthase
  7. Glutathione S-transferase Mu 2
  8. Glutathione peroxidase 7 precursor
  9. Epididymal secretory glutathione peroxidase precursor
  10. Glutathione S-transferase Mu 1
  11. Hydroxyacylglutathione hydrolase
  12. Glutathione S-transferase kappa 1
  13. Glutathione S-transferase Mu 3
  14. Glutathione S-transferase A1
  15. Maleylacetoacetate isomerase
  16. Glutathione S-transferase theta-2
  17. Glutathione S-transferase Mu 4
  18. Glutathione S-transferase Mu 5
  19. Microsomal glutathione S-transferase 2
  20. Glutathione transferase omega-1
  21. Glutathione S-transferase A5
  22. Glutathione S-transferase A2
  23. Glutathione peroxidase 6 precursor
  24. Glutathione S-transferase A3
  25. Glutathione S-transferase A4
  26. Glutathione peroxidase 1
  27. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
  28. Glutathione peroxidase 3 precursor
  29. Glutathione transferase omega-2
  30. Glutathione S-transferase theta-1
  31. Glutathione peroxidase 2
  32. Glutathione S-transferase P
  33. Glutathione-requiring prostaglandin D synthase
  34. RalA-binding protein 1
  35. Hydroxyacylglutathione hydrolase-like protein
  36. Gamma-glutamyltransferase 6 homolog
  37. Uncharacterized protein GSTZ1
  38. GGTL3 protein (Fragment)
  39. Gamma-glutamyltransferase-like activity 1
  40. Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
  41. cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
  42. LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
  43. cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
  44. cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum)
  45. cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
  46. cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
  47. cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
Enzyme 1 [top]
Enzyme 1 ID 5308
Enzyme 1 Name Prostaglandin E synthase
Enzyme 1 Synonyms
  1. Microsomal glutathione S- transferase 1-like 1
  2. MGST1-L1
  3. p53-induced apoptosis protein 12
Enzyme 1 Gene Name PTGES
Enzyme 1 Protein Sequence >Prostaglandin E synthase
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCR
SDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGK
LRAPIRSVTYTLAQLPCASMALQILWEAARHL
Enzyme 1 Number of Residues 152
Enzyme 1 Molecular Weight 17103
Enzyme 1 Theoretical pI 9.77
Enzyme 1 GO Classification Not Available
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15- hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15- dihydroxy-9-oxoprosta-5,13-dienoate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-31
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 2415308 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O14684 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PTGES_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >462 bp
ATGCCTGCCCACAGCCTGGTGATGAGCAGCCCGGCCCTCCCGGCCTTCCTGCTCTGCAGC
ACGCTGCTGGTCATCAAGATGTACGTGGTGGCCATCATCACGGGCCAAGTGAGGCTGCGG
AAGAAGGCCTTTGCCAACCCCGAGGATGCCCTGAGACACGGAGGAGGCCCCCAGTATTGC
AGGAGCGACCCCGACGTGGAACGCTGCCTCAGGGCCCACCGGAACGACATGGAGACCATC
TACCCCTTCCTTTTCCTGGGCTTCGTCTACTCCTTTCTGGGTCCTAACCCTTTTGTCGCC
TGGATGCACTTCCTGGTCTTCCTCGTGGGCCGTGTGGCACACACCGTGGCCTACCTGGGG
AAGCTGCGGGCACCCATCCGCTCCGTGACCTACACCCTGGCCCAGCTCCCCTGCGCCTCC
ATGGCTCTGCAGATCCTCTGGGAAGCGGCCCGCCACCTGTGA
Enzyme 1 GenBank Gene ID AF010316 Link Image
Enzyme 1 GeneCard ID PTGES Link Image
Enzyme 1 GenAtlas ID PTGES Link Image
Enzyme 1 HGNC ID HGNC:9599 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9q34.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature. 1997 Sep 18;389(6648):300-5. [PubMed Link Image]
  2. Jakobsson PJ, Thoren S, Morgenstern R, Samuelsson B: Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7220-5. [PubMed Link Image]
  3. Forsberg L, Leeb L, Thoren S, Morgenstern R, Jakobsson P: Human glutathione dependent prostaglandin E synthase: gene structure and regulation. FEBS Lett. 2000 Apr 7;471(1):78-82. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5428
Enzyme 2 Name Glutathione reductase, mitochondrial precursor
Enzyme 2 Synonyms
  1. GR
  2. GRase
Enzyme 2 Gene Name GSR
Enzyme 2 Protein Sequence >Glutathione reductase, mitochondrial precursor
MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAG
AVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHS
EFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDP
KPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAG
YIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK
TLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPP
IGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQ
GLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
Enzyme 2 Number of Residues 522
Enzyme 2 Molecular Weight 56258
Enzyme 2 Theoretical pI 8.66
Enzyme 2 GO Classification
Function
  • FAD binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • disulfide oxidoreductase activity
  • electron transporter activity
  • glutathione-disulfide reductase activity
  • nucleotide binding
  • oxidoreductase activity
  • purine nucleotide binding
  • transporter activity
Process
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • glutathione metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function RNA processing and modification
Enzyme 2 Specific Function Maintains high levels of reduced glutathione in the cytosol
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-37
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 31825 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00390 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GSHR_HUMAN Link Image
Enzyme 2 PDB ID 1BWC Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1440 bp
ATGGCCTGCAGGCAGGAGCCGCAGCCGCAGGGCCCGCCGCCCGCTGCTGGCGCCGTGGCC
TCCTATGACTACCTGGTGATCGGGGGCGGCTCGGGCGGGCTGGCCAGCGCGCGCAGGGCG
GCCGAGCTGGGTGCCAGGGCCGCCGTGGTGGAGAGCCACAAGCTGGGTGGCACTTGCGTG
AATGTTGGATGTGTACCCAAAAAGGTAATGTGGAACACAGCTGTCCACTCTGAATTCATG
CATGATCATGCTGATTATGGCTTTCCAAGTTGTGAGGGTAAATTCAATTGGCGTGTTATT
AAGGAAAAGCGGGATGCCTATGTGAGCCGCCTGAATGCCATCTATCAAAACAATCTCACC
AAGTCCCATATAGAAATCATCCGTGGCCATGCAGCCTTCACGAGTGATCCCAAGCCCACA
ATAGAGGTCAGTGGGAAAAAGTACACCGCCCCACACATCCTGATCGCCACAGGTGGTATG
CCCTCCACCCCTCATGAGAGCCAGATCCCCGGTGCCAGCTTAGGAATAACCAGCGATGGA
TTTTTTCAGCTGGAAGAATTGCCCGGCCGCAGCGTCATTGTTGGTGCAGGTTACATTGCT
GTGGAGATGGCAGGGATCCTGTCAGCCCTGGGTTCTAAGACATCACTGATGATACGGCAT
GATAAGGTACTTAGAAGTTTTGATTCAATGATCAGCACCAACTGCACGGAGGAGCTGGAG
AACGCTGGCGTGGAGGTGCTGAAGTTCTCCCAGGTCAAGGAGGTTAAAAAGACTTTGTCG
GGCTTGGAAGTCAGCATGGTTACTGCAGTTCCCGGTAGGCTACCAGTCATGACCATGATT
CCAGATGTTGACTGCCTGCTCTGGGCCATTGGGCGGGTCCCGAATACCAAGGACCTGAGT
TTAAACAAACTGGGGATTCAAACCGATGACAAGGGTCATATCATCGTAGACGAATTCCAG
AATACCAACGTCAAAGGCATCTATGCAGTTGGGGATGTATGTGGAAAAGCTCTTCTTACT
CCAGTTGCAATAGCTGCTGGCCGAAAACTTGCCCATCGACTTTTTGAATATAAGGAAGAT
TCCAAATTAGATTATAACAACATCCCAACTGTGGTCTTCAGCCACCCCCCTATTGGGACA
GTGGGACTCACGGAAGATGAAGCCATTCATAAATATGGAATAGAAAATGTGAAGACCTAT
TCAACGAGCTTTACCCCGATGTATCACGCAGTTACCAAAAGGAAAACAAAATGTGTGATG
AAAATGGTCTGTGCTAACAAGGAAGAAAAGGTGGTTGGGATCCATATGCAGGGACTTGGG
TGTGATGAAATGCTGCAGGGTTTTGCTGTTGCAGTGAAGATGGGAGCAACGAAGGCAGAC
TTTGACAACACAGTCGCCATTCACCCTACCTCTTCAGAAGAGCTGGTCACACTTCGTTGA
Enzyme 2 GenBank Gene ID X15722 Link Image
Enzyme 2 GeneCard ID GSR Link Image
Enzyme 2 GenAtlas ID GSR Link Image
Enzyme 2 HGNC ID HGNC:4623 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8p21.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Tutic M, Lu XA, Schirmer RH, Werner D: Cloning and sequencing of mammalian glutathione reductase cDNA. Eur J Biochem. 1990 Mar 30;188(3):523-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. Biochem Biophys Res Commun. 2000 Mar 16;269(2):366-8. [PubMed Link Image]
  3. Krauth-Siegel RL, Blatterspiel R, Saleh M, Schiltz E, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. Eur J Biochem. 1982 Jan;121(2):259-67. [PubMed Link Image]
  4. Krohne-Ehrich G, Schirmer RH, Untucht-Grau R: Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. Eur J Biochem. 1977 Oct 17;80(1):65-71. [PubMed Link Image]
  5. Thieme R, Pai EF, Schirmer RH, Schulz GE: Three-dimensional structure of glutathione reductase at 2 A resolution. J Mol Biol. 1981 Nov 15;152(4):763-82. [PubMed Link Image]
  6. Karplus PA, Schulz GE: Refined structure of glutathione reductase at 1.54 A resolution. J Mol Biol. 1987 Jun 5;195(3):701-29. [PubMed Link Image]
  7. Savvides SN, Karplus PA: Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. [PubMed Link Image]
  8. Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF: Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. [PubMed Link Image]
  9. Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5629
Enzyme 3 Name Lactoylglutathione lyase
Enzyme 3 Synonyms
  1. Methylglyoxalase
  2. Aldoketomutase
  3. Glyoxalase I
  4. Glx I
  5. Ketone-aldehyde mutase
  6. S-D- lactoylglutathione methylglyoxal lyase
Enzyme 3 Gene Name GLO1
Enzyme 3 Protein Sequence >Lactoylglutathione lyase
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQK
CDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNS
DPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKM
ATLM
Enzyme 3 Number of Residues 184
Enzyme 3 Molecular Weight 20778
Enzyme 3 Theoretical pI 4.92
Enzyme 3 GO Classification
Function
  • carbon-sulfur lyase activity
  • catalytic activity
  • lactoylglutathione lyase activity
  • lyase activity
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (R)-S-lactoylglutathione = glutathione + methylglyoxal
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 219664 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q04760 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LGUL_HUMAN Link Image
Enzyme 3 PDB ID 1QIP Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >555 bp
ATGGCAGAACCGCAGCCCCCGTCCGGCGGCCTCACGGACGAGGCCGCCCTCAGTTGCTGC
TCCGACGCGGACCCCAGTACCAAGGATTTTCTATTGCAGCAGACCATGCTACGAGTGAAG
GATCCTAAGAAGTCACTGGATTTTTATACTAGAGTTCTTGGAATGACGCTAATCCAAAAA
TGTGATTTTCCCATTATGAAGTTTTCACTCTACTTCTTGGCTTATGAGGATAAAAATGAC
ATCCCTAAAGAAAAAGATGAAAAAATAGCCTGGGCGCTCTCCAGAAAAGCTACACTTGAG
CTGACACACAATTGGGGCACTGAAGATGATGCGACCCAGAGTTACCACAATGGCAATTCA
GACCCTCGAGGATTCGGTCATATTGGAATTGCTGTTCCTGATGTATACAGTGCTTGTAAA
AGGTTTGAAGAACTGGGAGTCAAATTTGTGAAGAAACCTGATGATGGTAAAATGAAAGGC
CTGGCATTTATTCAAGATCCTGATGGCTACTGGATTGAAATTTTGAATCCTAACAAAATG
GCAACCTTAATGTAG
Enzyme 3 GenBank Gene ID D13315 Link Image
Enzyme 3 GeneCard ID GLO1 Link Image
Enzyme 3 GenAtlas ID GLO1 Link Image
Enzyme 3 HGNC ID HGNC:4323 Link Image
Enzyme 3 Chromosome Location 6
Enzyme 3 Locus 6p21.3-p21.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kim NS, Umezawa Y, Ohmura S, Kato S: Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J Biol Chem. 1993 May 25;268(15):11217-21. [PubMed Link Image]
  2. Ranganathan S, Walsh ES, Godwin AK, Tew KD: Cloning and characterization of human colon glyoxalase-I. J Biol Chem. 1993 Mar 15;268(8):5661-7. [PubMed Link Image]
  3. Ridderstrom M, Mannervik B: Optimized heterologous expression of the human zinc enzyme glyoxalase I. Biochem J. 1996 Mar 1;314 ( Pt 2):463-7. [PubMed Link Image]
  4. Ranganathan S, Ciaccio PJ, Walsh ES, Tew KD: Genomic sequence of human glyoxalase-I: analysis of promoter activity and its regulation. Gene. 1999 Nov 15;240(1):149-55. [PubMed Link Image]
  5. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  6. Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA: Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. EMBO J. 1997 Jun 16;16(12):3386-95. [PubMed Link Image]
  7. Ridderstrom M, Cameron AD, Jones TA, Mannervik B: Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I. J Biol Chem. 1998 Aug 21;273(34):21623-8. [PubMed Link Image]
  8. Cameron AD, Ridderstrom M, Olin B, Kavarana MJ, Creighton DJ, Mannervik B: Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry. 1999 Oct 12;38(41):13480-90. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6005
Enzyme 4 Name Gamma-glutamyltranspeptidase 1 precursor
Enzyme 4 Synonyms
  1. Gamma- glutamyltransferase 1
  2. GGT 1
  3. CD224 antigen[Contains: Gamma- glutamyltranspeptidase 1 heavy chain
  4. Gamma-glutamyltranspeptidase 1 light chain]
Enzyme 4 Gene Name GGT1
Enzyme 4 Protein Sequence >Gamma-glutamyltranspeptidase 1 precursor
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
Enzyme 4 Number of Residues 569
Enzyme 4 Molecular Weight 61411
Enzyme 4 Theoretical pI 7.14
Enzyme 4 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive
Enzyme 4 Pathways
Enzyme 4 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-30
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 183138 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P19440 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GGT1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1710 bp
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
Enzyme 4 GenBank Gene ID J04131 Link Image
Enzyme 4 GeneCard ID GGT1 Link Image
Enzyme 4 GenAtlas ID GGT1 Link Image
Enzyme 4 HGNC ID HGNC:4250 Link Image
Enzyme 4 Chromosome Location 22
Enzyme 4 Locus 22q11.23
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed Link Image]
  2. Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed Link Image]
  3. Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed Link Image]
  4. Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed Link Image]
  5. Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed Link Image]
  6. Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed Link Image]
  7. Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed Link Image]
  8. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  9. Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed Link Image]
  10. Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed Link Image]
  11. Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed Link Image]
  12. Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed Link Image]
  13. Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed Link Image]
  14. Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed Link Image]
  15. Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed Link Image]
  16. Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6071
Enzyme 5 Name Glutathione synthetase
Enzyme 5 Synonyms
  1. Glutathione synthase
  2. GSH synthetase
  3. GSH-S
Enzyme 5 Gene Name GSS
Enzyme 5 Protein Sequence >Glutathione synthetase
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
Enzyme 5 Number of Residues 474
Enzyme 5 Molecular Weight 52385
Enzyme 5 Theoretical pI 5.73
Enzyme 5 GO Classification
Function
  • ATP binding
  • acid-amino acid ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • glutathione synthase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • glutathione biosynthesis
  • glutathione metabolism
  • metabolism
  • physiological process
Component
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 886284 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P48637 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GSHB_HUMAN Link Image
Enzyme 5 PDB ID 2HGS Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1425 bp
ATGGCCACCAACTGGGGGAGCCTCTTGCAGGATAAACAGCAGCTAGAGGAGCTGGCACGG
CAGGCCGTGGACCGGGCCCTGGCTGAGGGAGTATTGCTGAGGACCTCACAGGAGCCCACT
TCCTCGGAGGTGGTGAGCTATGCCCCATTCACGCTCTTCCCCTCACTGGTCCCCAGTGCC
CTGCTGGAGCAAGCCTATGCTGTGCAGATGGACTTCAACCTGCTAGTGGATGCTGTCAGC
CAGAACGCTGCCTTCCTGGAGCAAACTCTTTCCAGCACCATCAAACAGGATGACTTTACC
GCTCGTCTCTTTGACATCCACAAGCAAGTCCTAAAAGAGGGCATTGCCCAGACTGTGTTC
CTGGGCCTGAATCGCTCAGACTACATGTTCCAGCGCAGCGCAGATGGCTCCCCAGCCCTG
AAACAGATCGAAATCAACACCATCTCTGCCAGCTTTGGGGGCCTGGCCTCCCGGACCCCA
GCTGTGCACCGACATGTTCTCAGTGTCCTGAGTAAGACCAAAGAAGCTGGCAAGATCCTC
TCTAATAATCCCAGCAAGGGACTGGCCCTGGGAATTGCCAAAGCCTGGGAGCTCTACGGC
TCACCCAATGCTCTGGTGCTACTGATTGCTCAAGAGAAGGAAAGAAACATATTTGACCAG
CGTGCCATAGAGAATGAGCTACTGGCCAGGAACATCCATGTGATCCGACGAACATTTGAA
GATATCTCTGAAAAGGGGTCTCTGGACCAAGACCGAAGGCTGTTTGTGGATGGCCAGGAA
ATTGCTGTGGTTTACTTCCGGGATGGCTACATGCCTCGTCAGTACAGTCTACAGAATTGG
GAAGCACGTCTACTGCTGGAGAGGTCACATGCTGCCAAGTGCCCAGACATTGCCACCCAG
CTGGCTGGGACTAAGAAGGTGCAGCAGGAGCTAAGCAGGCCGGGCATGCTGGAGATGTTG
CTCCCTGGCCAGCCTGAGGCTGTGGCCCGCCTCCGCGCCACCTTTGCTGGCCTCTACTCA
CTGGATGTGGGTGAAGAAGGGGACCAGGCCATCGCCGAGGCCCTTGCTGCCCCTAGCCGG
TTTGTGCTAAAGCCCCAGAGAGAGGGTGGAGGTAACAACCTATATGGGGAGGAAATGGTA
CAGGCCCTGAAACAGCTGAAGGACAGTGAGGAGAGGGCCTCCTACATCCTCATGGAGAAG
ATCGAACCTGAGCCTTTTGAGAATTGCCTGCTACGGCCTGGCAGCCCTGCCCGAGTGGTC
CAGTGCATTTCAGAGCTGGGCATCTTTGGGGTCTATGTCAGGCAGGAAAAGACACTCGTG
ATGAACAAGCACGTGGGGCATCTACTTCGAACCAAAGCCATCGAGCATGCAGATGGTGGT
GTGGCAGCGGGAGTGGCAGTCCTGGACAACCCATACCCTGTGTGA
Enzyme 5 GenBank Gene ID L42531 Link Image
Enzyme 5 GeneCard ID GSS Link Image
Enzyme 5 GenAtlas ID GSS Link Image
Enzyme 5 HGNC ID HGNC:4624 Link Image
Enzyme 5 Chromosome Location 20
Enzyme 5 Locus 20q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Gali RR, Board PG: Sequencing and expression of a cDNA for human glutathione synthetase. Biochem J. 1995 Aug 15;310 ( Pt 1):353-8. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Shi ZZ, Habib GM, Rhead WJ, Gahl WA, He X, Sazer S, Lieberman MW: Mutations in the glutathione synthetase gene cause 5-oxoprolinuria. Nat Genet. 1996 Nov;14(3):361-5. [PubMed Link Image]
  4. Dahl N, Pigg M, Ristoff E, Gali R, Carlsson B, Mannervik B, Larsson A, Board P: Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction. Hum Mol Genet. 1997 Jul;6(7):1147-52. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6087
Enzyme 6 Name Leukotriene C4 synthase
Enzyme 6 Synonyms
  1. Leukotriene-C(4synthase
  2. LTC4 synthase
Enzyme 6 Gene Name LTC4S
Enzyme 6 Protein Sequence >Leukotriene C4 synthase
MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYF
PLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVA
LAALGLLAHFLPAALRAALLGRLRTLLPWA
Enzyme 6 Number of Residues 150
Enzyme 6 Molecular Weight 16567
Enzyme 6 Theoretical pI 10.40
Enzyme 6 GO Classification
Function
  • enzyme activator activity
  • enzyme regulator activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • icosanoid metabolism
  • leukotriene metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4
Enzyme 6 Pathways
Enzyme 6 Reactions
  • leukotriene C4 = leukotriene A4 + glutathione
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-23
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 520485 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q16873 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name LTC4S_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >453 bp
ATGAAGGACGAGGTAGCTCTACTGGCTGCTGTCACCCTCCTGGGAGTCCTGCTGCAAGCC
TACTTCTCCCTGCAGGTGATCTCGGCGCGCAGGGCCTTCCGCGTGTCGCCGCCGCTCACC
ACCGGCCCACCCGAGTTCGAGCGCGTCTACCGAGCCCAGGTGAACTGCAGCGAGTACTTC
CCGCTGTTCCTCGCCACGCTCTGGGTCGCCGGCATCTTCTTTCATGAAGGGGCGGCGGCC
CTGTGCGGCCTGGTCTACCTGTTCGCGCGCCTCCGCTACTTCCAGGGCTACGCGCGCTCC
GCGCAGCTCAGGCTGGCACCGCTGTACGCGAGCGCGCGCGCCCTCTGGCTGCTGGTGGCG
CTGGCTGCGCTCGGCCTGCTCGCCCACTTCCTCCCGGCCGCGCTGCGCGCCGCGCTCCTC
GGACGGCTCCGGACGCTGCTGCCGTGGGCCTGA
Enzyme 6 GenBank Gene ID U09353 Link Image
Enzyme 6 GeneCard ID LTC4S Link Image
Enzyme 6 GenAtlas ID LTC4S Link Image
Enzyme 6 HGNC ID HGNC:6719 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q35
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Lam BK, Penrose JF, Freeman GJ, Austen KF: Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7663-7. [PubMed Link Image]
  2. Welsch DJ, Creely DP, Hauser SD, Mathis KJ, Krivi GG, Isakson PC: Molecular cloning and expression of human leukotriene-C4 synthase. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9745-9. [PubMed Link Image]
  3. Penrose JF, Spector J, Baldasaro M, Xu K, Boyce J, Arm JP, Austen KF, Lam BK: Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. J Biol Chem. 1996 May 10;271(19):11356-61. [PubMed Link Image]
  4. Bigby TD, Hodulik CR, Arden KC, Fu L: Molecular cloning of the human leukotriene C4 synthase gene and assignment to chromosome 5q35. Mol Med. 1996 Sep;2(5):637-46. [PubMed Link Image]
  5. Nicholson DW, Ali A, Vaillancourt JP, Calaycay JR, Mumford RA, Zamboni RJ, Ford-Hutchinson AW: Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):2015-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6088
Enzyme 7 Name Glutathione S-transferase Mu 2
Enzyme 7 Synonyms
  1. GSTM2-2
  2. GST class-mu 2
Enzyme 7 Gene Name GSTM2
Enzyme 7 Protein Sequence >Glutathione S-transferase Mu 2
MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDF
EKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK
Enzyme 7 Number of Residues 218
Enzyme 7 Molecular Weight 25745
Enzyme 7 Theoretical pI 6.29
Enzyme 7 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 7 Pathways
Enzyme 7 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-16
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 183301 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P28161 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GSTM2_HUMAN Link Image
Enzyme 7 PDB ID 1XW5 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >657 bp
ATGCCCATGACACTGGGGTACTGGAACATCCGCGGGCTGGCCCATTCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGACTCACAAGATCACCCAGAGCAATGCCATCCTGCGGTACATT
GCCCGCAAGCACAACCTGTGCGGGGAATCAGAAAAGGAGCAGATTCGCGAAGACATTTTG
GAGAACCAGTTTATGGACAGCCGTATGCAGCTGGCCAAACTCTGCTATGACCCAGATTTT
GAGAAACTGAAACCAGAATACCTGCAGGCACTCCCTGAAATGCTGAAGCTCTACTCACAG
TTTCTGGGGAAGCAGCCATGGTTTCTTGGGGACAAGATCACCTTTGTGGATTTCATCGCT
TATGATGTCCTTGAGAGAAACCAAGTATTTGAGCCCAGCTGCCTGGATGCCTTCCCAAAC
CTGAAGGACTTCATCTCCCGATTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCACAAAGATGGCTGTCTGGGGCAACAAGTAG
Enzyme 7 GenBank Gene ID M63509 Link Image
Enzyme 7 GeneCard ID GSTM2 Link Image
Enzyme 7 GenAtlas ID GSTM2 Link Image
Enzyme 7 HGNC ID HGNC:4634 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1p13.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Vorachek WR, Pearson WR, Rule GS: Cloning, expression, and characterization of a class-mu glutathione transferase from human muscle, the product of the GST4 locus. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4443-7. [PubMed Link Image]
  2. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed Link Image]
  3. Raghunathan S, Chandross RJ, Kretsinger RH, Allison TJ, Penington CJ, Rule GS: Crystal structure of human class mu glutathione transferase GSTM2-2. Effects of lattice packing on conformational heterogeneity. J Mol Biol. 1994 May 20;238(5):815-32. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6089
Enzyme 8 Name Glutathione peroxidase 7 precursor
Enzyme 8 Synonyms
  1. CL683
Enzyme 8 Gene Name GPX7
Enzyme 8 Protein Sequence >Glutathione peroxidase 7 precursor
MVAATVAAAWLLLWAAACAQQEQDFYDFKAVNIRGKLVSLEKYRGSVSLVVNVASECGFT
DQHYRALQQLQRDLGPHHFNVLAFPCNQFGQQEPDSNKEIESFARRTYSVSFPMFSKIAV
TGTGAHPAFKYLAQTSGKEPTWNFWKYLVAPDGKVVGAWDPTVSVEEVRPQITALVRKLI
LLKREDL
Enzyme 8 Number of Residues 187
Enzyme 8 Molecular Weight 20996
Enzyme 8 Theoretical pI 8.46
Enzyme 8 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 8 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 8 Specific Function 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Enzyme 8 Pathways
Enzyme 8 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 25990366 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q96SL4 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GPX7_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >564 bp
ATGGTGGCGGCGACGGTGGCAGCGGCGTGGCTGCTCCTGTGGGCTGCGGCCTGCGCGCAG
CAGGAGCAGGACTTCTACGACTTCAAGGCGGTCAACATCCGGGGCAAACTGGTGTCGCTG
GAGAAGTACCGCGGATCGGTGTCCCTGGTGGTGAATGTGGCCAGCGAGTGCGGCTTCACA
GACCAGCACTACCGAGCCCTGCAGCAGCTGCAGCGAGACCTGGGCCCCCACCACTTTAAC
GTGCTCGCCTTCCCCTGCAACCAGTTTGGCCAACAGGAGCCTGACAGCAACAAGGAGATT
GAGAGCTTTGCCCGCCGCACCTACAGTGTCTCATTCCCCATGTTTAGCAAGATTGCAGTC
ACCGGTACTGGTGCCCATCCTGCCTTCAAGTACCTGGCCCAGACTTCTGGGAAGGAGCCC
ACCTGGAACTTCTGGAAGTACCTAGTAGCCCCAGATGGAAAGGTGGTAGGGGCTTGGGAC
CCAACTGTGTCAGTGGAGGAGGTCAGACCCCAGATCACAGCGCTCGTGAGGAAGCTCATC
CTACTGAAGCGAGAAGACTTATAA
Enzyme 8 GenBank Gene ID AF320068 Link Image
Enzyme 8 GeneCard ID GPX7 Link Image
Enzyme 8 GenAtlas ID GPX7 Link Image
Enzyme 8 HGNC ID HGNC:4559 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p32
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6090
Enzyme 9 Name Epididymal secretory glutathione peroxidase precursor
Enzyme 9 Synonyms
  1. Epididymis-specific glutathione peroxidase-like protein
  2. EGLP
Enzyme 9 Gene Name GPX5
Enzyme 9 Protein Sequence >Epididymal secretory glutathione peroxidase precursor
MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYV
GKHILFVNVATYCGLTAQYPELNALQEELKPYGLVVLGFPCNQFGKQEPGDNKEILPGLK
YVRPGGGFVPSFQLFEKGDVNGEKEQKVFSFLKHSCPHPSEILGTFKSISWDPVKVHDIR
WNFEKFLVGPDGIPVMRWSHRATVSSVKTDILAYLKQFKTK
Enzyme 9 Number of Residues 221
Enzyme 9 Molecular Weight 25203
Enzyme 9 Theoretical pI 8.89
Enzyme 9 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 9 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 9 Specific Function Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathionine peroxidase-like protective system against peroxide damage in sperm membrane lipids
Enzyme 9 Pathways
Enzyme 9 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-21
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3288455 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75715 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name GPX5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >666 bp
ATGACTACACAGTTAAGGGTCGTCCATCTGCTTCCCCTTCTCCTAGCCTGCTTTGTGCAA
ACAAGTCCCAAGCAGGAGAAGATGAAGATGGATTGCCACAAAGACGAGAAAGGCACCATC
TATGACTATGAGGCCATCGCACTTAATAAGAATGAATATGTTTCCTTCAAGCAGTATGTG
GGCAAGCACATCCTCTTCGTCAACGTGGCCACCTACTGTGGTCTGACAGCGCAATATCCT
GAACTAAATGCACTCCAGGAGGAGCTGAAGCCCTATGGTCTAGTTGTGTTGGGCTTTCCC
TGCAACCAATTTGGAAAGCAAGAACCAGGAGATAACAAAGAGATTCTTCCTGGGCTCAAG
TATGTCCGTCCAGGGGGAGGATTTGTACCTAGTTTCCAGCTTTTTGAGAAAGGGGATGTG
AATGGTGAAAAAGAACAGAAAGTCTTCAGTTTCTTGAAGCACTCCTGTCCTCATCCCTCT
GAGATTTTGGGCACATTCAAATCTATATCCTGGGACCCTGTAAAGGTCCATGACATCCGT
TGGAACTTTGAAAAGTTCCTGGTGGGGCCTGATGGAATCCCTGTCATGCGCTGGTCCCAC
CGGGCTACGGTCAGCTCAGTCAAGACAGACATCCTGGCGTACTTGAAGCAATTCAAAACC
AAATAG
Enzyme 9 GenBank Gene ID AJ005277 Link Image
Enzyme 9 GeneCard ID GPX5 Link Image
Enzyme 9 GenAtlas ID GPX5 Link Image
Enzyme 9 HGNC ID HGNC:4557 Link Image
Enzyme 9 Chromosome Location 6
Enzyme 9 Locus 6p22.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Hall L, Williams K, Perry AC, Frayne J, Jury JA: The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. Biochem J. 1998 Jul 1;333 ( Pt 1):5-9. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6091
Enzyme 10 Name Glutathione S-transferase Mu 1
Enzyme 10 Synonyms
  1. GSTM1-1
  2. GST class-mu 1
  3. GSTM1a-1a
  4. GSTM1b-1b
  5. HB subunit 4
  6. GTH4
Enzyme 10 Gene Name GSTM1
Enzyme 10 Protein Sequence >Glutathione S-transferase Mu 1
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
Enzyme 10 Number of Residues 218
Enzyme 10 Molecular Weight 25712
Enzyme 10 Theoretical pI 6.67
Enzyme 10 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 10 Pathways
Enzyme 10 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-16
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 31924 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P09488 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GSTM1_HUMAN Link Image
Enzyme 10 PDB ID 1XWK Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >657 bp
ATGCCCATGATACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTATGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCTTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGACCATGGACAACCATATGCAGCTGGGCATGATCTGCTACAATCCAGAATTT
GAGAAACTGAAGCCAAAGTACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAAACAAGATCACTTTTGTAGATTTTCTCGTC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCTCAAAGATGGCTGTCTGGGGCAACAAGTAG
Enzyme 10 GenBank Gene ID X08020 Link Image
Enzyme 10 GeneCard ID GSTM1 Link Image
Enzyme 10 GenAtlas ID GSTM1 Link Image
Enzyme 10 HGNC ID HGNC:4632 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p13.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. DeJong JL, Chang CM, Whang-Peng J, Knutsen T, Tu CP: The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA. Nucleic Acids Res. 1988 Sep 12;16(17):8541-54. [PubMed Link Image]
  2. Seidegard J, Vorachek WR, Pero RW, Pearson WR: Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7293-7. [PubMed Link Image]
  3. Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed Link Image]
  4. Comstock KE, Sanderson BJ, Claflin G, Henner WD: GST1 gene deletion determined by polymerase chain reaction. Nucleic Acids Res. 1990 Jun 25;18(12):3670. [PubMed Link Image]
  5. Pearson WR, Vorachek WR, Xu SJ, Berger R, Hart I, Vannais D, Patterson D: Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13. Am J Hum Genet. 1993 Jul;53(1):220-33. [PubMed Link Image]
  6. Tsuchida S, Maki T, Sato K: Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. Multiplicity of the human class Mu forms. J Biol Chem. 1990 May 5;265(13):7150-7. [PubMed Link Image]
  7. Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed Link Image]
  8. Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed Link Image]
  9. Singhal SS, Ahmad H, Sharma R, Gupta S, Haque AK, Awasthi YC: Purification and characterization of human muscle glutathione S-transferases: evidence that glutathione S-transferase zeta corresponds to a locus distinct from GST1, GST2, and GST3. Arch Biochem Biophys. 1991 Feb 15;285(1):64-73. [PubMed Link Image]
  10. Singhal SS, Saxena M, Awasthi S, Ahmad H, Sharma R, Awasthi YC: Gender related differences in the expression and characteristics of glutathione S-transferases of human colon. Biochim Biophys Acta. 1992 Nov 15;1171(1):19-26. [PubMed Link Image]
  11. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
  12. Patskovsky YV, Patskovska LN, Listowsky I: Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a. Biochemistry. 1999 Jan 26;38(4):1193-202. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6092
Enzyme 11 Name Hydroxyacylglutathione hydrolase
Enzyme 11 Synonyms
  1. Glyoxalase II
  2. GLX II
Enzyme 11 Gene Name HAGH
Enzyme 11 Protein Sequence >Hydroxyacylglutathione hydrolase
MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHA
GGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS
KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNL
KFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD
PVTTMRAVRREKDQFKMPRD
Enzyme 11 Number of Residues 260
Enzyme 11 Molecular Weight 28860
Enzyme 11 Theoretical pI 7.36
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Thiolesterase that catalyzes the hydrolysis of S-D- lactoyl-glutathione to form glutathione and D-lactic acid
Enzyme 11 Pathways
Enzyme 11 Reactions
  • S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 1237213 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q16775 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name GLO2_HUMAN Link Image
Enzyme 11 PDB ID 1QH3 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >783 bp
ATGAAGGTAGAGGTGCTGCCTGCCCTGACCGACAACTACATGTACCTGGTCATTGATGAT
GAGACCAAGGAGGCTGCCATTGTGGATCCGGTGCAGCCCCAGAAGGTCGTGGACGCGGCG
AGAAAGCACGGGGTGAAACTGACCACAGTGCTCACCACCCACCACCACTGGGACCATGCT
GGCGGGAATGAGAAACTGGTCAAGCTGGAGTCGGGACTGAAGGTGTACGGGGGTGACGAC
CGTATCGGGGCCCTGACTCACAAGATCACTCACCTGTCCACACTGCAGGTGGGGTCTCTG
AACGTCAAGTGCCTGGCGACCCCGTGCCACACTTCAGGACACATTTGTTACTTCGTGAGC
AAGCCCGGAGGCTCGGAGCCCCCTGCCGTGTTCACAGGTGACACCTTGTTTGTGGCTGGC
TGCGGGAAGTTCTATGAAGGGACTGCGGATGAGATGTGTAAAGCTCTGCTGGAGGTCTTG
GGCCGGCTCCCCCCGGACACAAGAGTCTACTGTGGCCACGAGTACACCATCAACAACCTC
AAGTTTGCACGCCACGTGGAGCCCGGCAATGCCGCCATCCGGGAGAAGCTGGCCTGGGCC
AAGGAGAAGTACAGCATCGGGGAGCCCACAGTGCCATCCACCCTGGCAGAGGAGTTTACC
TACAACCCCTTCATGAGAGTGAGGGAGAAGACGGTGCAGCAGCACGCAGGTGAGACGGAC
CCGGTGACCACCATGCGGGCCGTGCGCAGGGAGAAGGACCAGTTCAAGATGCCCCGGGAC
TGA
Enzyme 11 GenBank Gene ID X90999 Link Image
Enzyme 11 GeneCard ID HAGH Link Image
Enzyme 11 GenAtlas ID HAGH Link Image
Enzyme 11 HGNC ID HGNC:4805 Link Image
Enzyme 11 Chromosome Location 16
Enzyme 11 Locus 16p13.3
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Ridderstrom M, Saccucci F, Hellman U, Bergman T, Principato G, Mannervik B: Molecular cloning, heterologous expression, and characterization of human glyoxalase II. J Biol Chem. 1996 Jan 5;271(1):319-23. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Cameron AD, Ridderstrom M, Olin B, Mannervik B: Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6093
Enzyme 12 Name Glutathione S-transferase kappa 1
Enzyme 12 Synonyms
  1. GST 13-13
  2. Glutathione S-transferase subunit 13
  3. GST class-kappa
  4. GSTK1-1
  5. hGSTK1
Enzyme 12 Gene Name GSTK1
Enzyme 12 Protein Sequence >Glutathione S-transferase kappa 1
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
Enzyme 12 Number of Residues 226
Enzyme 12 Molecular Weight 25497
Enzyme 12 Theoretical pI 8.69
Enzyme 12 GO Classification
Function
  • catalytic activity
  • disulfide oxidoreductase activity
  • oxidoreductase activity
  • protein disulfide oxidoreductase activity
Process
Component
  • cell
  • periplasmic space
  • periplasmic space (sensu Gram-negative Bacteria)
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB)
Enzyme 12 Pathways
Enzyme 12 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 41351794 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y2Q3 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GSTK1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
Enzyme 12 GenBank Gene ID AY520571 Link Image
Enzyme 12 GeneCard ID GSTK1 Link Image
Enzyme 12 GenAtlas ID GSTK1 Link Image
Enzyme 12 HGNC ID HGNC:16906 Link Image
Enzyme 12 Chromosome Location 7
Enzyme 12 Locus -
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6095
Enzyme 13 Name Glutathione S-transferase Mu 3
Enzyme 13 Synonyms
  1. GSTM3-3
  2. GST class-mu 3
  3. hGSTM3-3
Enzyme 13 Gene Name GSTM3
Enzyme 13 Protein Sequence >Glutathione S-transferase Mu 3
MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLD
FPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCY
SSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLD
EFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
Enzyme 13 Number of Residues 225
Enzyme 13 Molecular Weight 26560
Enzyme 13 Theoretical pI 5.19
Enzyme 13 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Not Available
Enzyme 13 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May govern uptake and detoxification of both endogenous compounds and xenobiotics at the testis and brain blood barriers
Enzyme 13 Pathways
Enzyme 13 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 306820 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P21266 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name GSTM3_HUMAN Link Image
Enzyme 13 PDB ID 3GTU Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >678 bp
ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA
Enzyme 13 GenBank Gene ID J05459 Link Image
Enzyme 13 GeneCard ID GSTM3 Link Image
Enzyme 13 GenAtlas ID GSTM3 Link Image
Enzyme 13 HGNC ID HGNC:4635 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p13.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Campbell E, Takahashi Y, Abramovitz M, Peretz M, Listowsky I: A distinct human testis and brain mu-class glutathione S-transferase. Molecular cloning and characterization of a form present even in individuals lacking hepatic type mu isoenzymes. J Biol Chem. 1990 Jun 5;265(16):9188-93. [PubMed Link Image]
  2. Patskovsky YV, Huang MQ, Takayama T, Listowsky I, Pearson WR: Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster. Arch Biochem Biophys. 1999 Jan 1;361(1):85-93. [PubMed Link Image]
  3. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed Link Image]
  4. Hussey AJ, Hayes JD: Human Mu-class glutathione S-transferases present in liver, skeletal muscle and testicular tissue. Biochim Biophys Acta. 1993 Nov 10;1203(1):131-41. [PubMed Link Image]
  5. Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6096
Enzyme 14 Name Glutathione S-transferase A1
Enzyme 14 Synonyms
  1. GTH1
  2. HA subunit 1
  3. GST- epsilon
  4. GSTA1-1
  5. GST class-alpha member 1
Enzyme 14 Gene Name GSTA1
Enzyme 14 Protein Sequence >Glutathione S-transferase A1
MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAK
LALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF
Enzyme 14 Number of Residues 222
Enzyme 14 Molecular Weight 25631
Enzyme 14 Theoretical pI 9.34
Enzyme 14 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 14 Pathways
Enzyme 14 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 306809 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P08263 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GSTA1_HUMAN Link Image
Enzyme 14 PDB ID 1K3Y Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTTCAATGCACGGGGCAGAATGGAGTCCACCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAGAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTCCTTCTGCCCGTATGTCCACCTGAGGAAAAAGATGCCAAG
CTTGCCTTGATCAAGGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCATCTG
GTGGAACTTCTCTACTACGTCGAGGAGCTTGACTCCAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 14 GenBank Gene ID M15872 Link Image
Enzyme 14 GeneCard ID GSTA1 Link Image
Enzyme 14 GenAtlas ID GSTA1 Link Image
Enzyme 14 HGNC ID HGNC:4626 Link Image
Enzyme 14 Chromosome Location 6
Enzyme 14 Locus 6p12.1
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Tu CP, Qian B: Human liver glutathione S-transferases: complete primary sequence of an Ha subunit cDNA. Biochem Biophys Res Commun. 1986 Nov 26;141(1):229-37. [PubMed Link Image]
  2. Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed Link Image]
  3. Tu CP, Qian B: Nucleotide sequence of the human liver glutathione S-transferase subunit 1 cDNA. Biochem Soc Trans. 1987 Aug;15(4):734-6. [PubMed Link Image]
  4. Board PG, Webb GC: Isolation of a cDNA clone and localization of human glutathione S-transferase 2 genes to chromosome band 6p12. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2377-81. [PubMed Link Image]
  5. Rozen F, Nguyen T, Pickett CB: Isolation and characterization of a human glutathione S-transferase Ha1 subunit gene. Arch Biochem Biophys. 1992 Feb 1;292(2):589-93. [PubMed Link Image]
  6. Chow NW, Whang-Peng J, Kao-Shan CS, Tam MF, Lai HC, Tu CP: Human glutathione S-transferases. The Ha multigene family encodes products of different but overlapping substrate specificities. J Biol Chem. 1988 Sep 15;263(26):12797-800. [PubMed Link Image]
  7. Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed Link Image]
  8. Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed Link Image]
  9. Board PG, Mannervik B: The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase. Biochem J. 1991 Apr 1;275 ( Pt 1):171-4. [PubMed Link Image]
  10. Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al.: Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. J Mol Biol. 1993 Jul 5;232(1):192-212. [PubMed Link Image]
  11. Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA: Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. Structure. 1995 Jul 15;3(7):717-27. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6097
Enzyme 15 Name Maleylacetoacetate isomerase
Enzyme 15 Synonyms
  1. MAAI
  2. Glutathione S- transferase zeta 1
  3. GSTZ1-1
Enzyme 15 Gene Name GSTZ1
Enzyme 15 Protein Sequence >Maleylacetoacetate isomerase
MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVP
TLKIDGITIHQSLAIIEYLEETRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLK
QVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDL
TPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
Enzyme 15 Number of Residues 216
Enzyme 15 Molecular Weight 24182
Enzyme 15 Theoretical pI 8.71
Enzyme 15 GO Classification
Function
  • catalytic activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 15 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 15 Specific Function Bifunctional enzyme showing minimal glutathione- conjugating activity with ethacrynic acid and 7-chloro-4- nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T- butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid
Enzyme 15 Pathways
Enzyme 15 Reactions
  • 4-maleylacetoacetate = 4-fumarylacetoacetate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 2832731 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O43708 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name MAAI_HUMAN Link Image
Enzyme 15 PDB ID 1FW1 Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >651 bp
ATGCAGGCGGGGAAGCCCATCCTCTATTCCTATTTCCGAAGCTCCTGCTCATGGAGAGTT
CGAATTGCTCTGGCCTTGAAAGGCATCGACTACAAGACGGTGCCCATCAATCTCATAAAG
GATGGGGGCCAACAGTTTTCTAAGGACTTCCAGGCACTGAATCCTATGAAGCAGGTGCCA
ACCCTGAAGATTGATGGAATCACCATTCACCAGTCACTGGCCATCATTGAGTATCTAGAG
GAGACGCGTCCCACTCCGCGACTTCTGCCTCAGGACCCAAAGAAGAGGGCCAGCGTGCGT
ATGATTTCTGACCTCATCGCTGGTGGCATCCAGCCCCTGCAGAACCTGTCTGTCCTGAAG
CAAGTGGGAGAGGAGATGCAGCTGACCTGGGCCCAGAACGCCATCACTTGTGGCTTTAAC
GCCCTGGAGCAGATCCTACAGAGCACAGCGGGCATATACTGTGTAGGAGACGAGGTGACC
ATGGCTGATCTGTGCTTGGTGCCTCAGGTGGCAAATGCTGAAAGATTCAAGGTGGATCTC
ACCCCCTACCCTACCATCAGCTCCATCAACAAGAGGCTGCTGGTCTTGGAGGCCTTCCAG
GTGTCTCACCCCTGCCGGCAGCCAGATACACCCACTGAGCTGAGGGCCTAG
Enzyme 15 GenBank Gene ID AJ001838 Link Image
Enzyme 15 GeneCard ID GSTZ1 Link Image
Enzyme 15 GenAtlas ID GSTZ1 Link Image
Enzyme 15 HGNC ID HGNC:4643 Link Image
Enzyme 15 Chromosome Location 14
Enzyme 15 Locus 14q24.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Fernandez-Canon JM, Penalva MA: Characterization of a fungal maleylacetoacetate isomerase gene and identification of its human homologue. J Biol Chem. 1998 Jan 2;273(1):329-37. [PubMed Link Image]
  2. Board PG, Baker RT, Chelvanayagam G, Jermiin LS: Zeta, a novel class of glutathione transferases in a range of species from plants to humans. Biochem J. 1997 Dec 15;328 ( Pt 3):929-35. [PubMed Link Image]
  3. Blackburn AC, Woollatt E, Sutherland GR, Board PG: Characterization and chromosome location of the gene GSTZ1 encoding the human Zeta class glutathione transferase and maleylacetoacetate isomerase. Cytogenet Cell Genet. 1998;83(1-2):109-14. [PubMed Link Image]
  4. Fernandez-Canon JM, Hejna J, Reifsteck C, Olson S, Grompe M: Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase. Genomics. 1999 Jun 15;58(3):263-9. [PubMed Link Image]
  5. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  6. Tong Z, Board PG, Anders MW: Glutathione transferase zeta catalyses the oxygenation of the carcinogen dichloroacetic acid to glyoxylic acid. Biochem J. 1998 Apr 15;331 ( Pt 2):371-4. [PubMed Link Image]
  7. Blackburn AC, Tzeng HF, Anders MW, Board PG: Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis. Pharmacogenetics. 2000 Feb;10(1):49-57. [PubMed Link Image]
  8. Polekhina G, Board PG, Blackburn AC, Parker MW: Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry. 2001 Feb 13;40(6):1567-76. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6098
Enzyme 16 Name Glutathione S-transferase theta-2
Enzyme 16 Synonyms
  1. GST class-theta-2
Enzyme 16 Gene Name GSTT2
Enzyme 16 Protein Sequence >Glutathione S-transferase theta-2
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDG
DFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLG
PLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALG
YELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRI
ARIP
Enzyme 16 Number of Residues 244
Enzyme 16 Molecular Weight 27507
Enzyme 16 Theoretical pI 6.36
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 16 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity
Enzyme 16 Pathways
Enzyme 16 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-16
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 601918 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P30712 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name GSTT2_HUMAN Link Image
Enzyme 16 PDB ID 3LJR Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >735 bp
ATGGGCCTAGAGCTGTTTCTTGACCTGGTGTCCCAGCCCAGCCGCGCCGTCTACATCTTC
GCCAAGAAGAATGGCATCCCCTTAGAGCTGCGCACCGTGGATTTGGTCAAAGGGCAGCAC
AAGAGCAAGGAGTTCTTGCAGATCAACAGCCTGGGGAAACTGCCGACGCTCAAGGATGGT
GATTTCATCTTGACCGAAAGCTCGGCCATCCTGATTTACCTGAGCTGTAAGTACCAGACG
CCGGACCACTGGTATCCATCTGACCTGCAGGCTCGTGCCCGTGTTCATGAGTACCTGGGC
TGGCATGCCGACTGCATCCGTGGCACCTTTGGTATACCCCTGTGGGTCCAGGTGTTGGGG
CCACTCATTGGGGTCCAGGTGCCCGAGGAGAAGGTGGAACGCAACAGGACTGCCATGGAC
CAGGCCCTGCAATGGCTGGAGGACAAGTTCCTGGGGGACAGGCCCTTCCTCGCTGGCCAG
CAGGTGACACTGGCTGATCTCATGGCCCTGGAGGAGCTGATGCAGCCGGTGGCTCTCGGC
TACGAACTGTTTGAGGGACGGCCACGACTGGCAGCATGGCGTGGACGAGTGGAGGCTTTC
CTGGGTGCTGAGCTATGCCAGGAGGCCCACAGCATCATCTTGAGCATCCTGGAACAGGCG
GCCAAGAAAACCCTCCCAACACCCTCACCAGAGGCCTATCAGGCTATGCTGCTTCGAATC
GCCAGGATCCCCTGA
Enzyme 16 GenBank Gene ID L38503 Link Image
Enzyme 16 GeneCard ID GSTT2 Link Image
Enzyme 16 GenAtlas ID GSTT2 Link Image
Enzyme 16 HGNC ID HGNC:4642 Link Image
Enzyme 16 Chromosome Location 22
Enzyme 16 Locus 22q11.2|22q11.23
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Tan KL, Webb GC, Baker RT, Board PG: Molecular cloning of a cDNA and chromosomal localization of a human theta-class glutathione S-transferase gene (GSTT2) to chromosome 22. Genomics. 1995 Jan 20;25(2):381-7. [PubMed Link Image]
  2. Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Hussey AJ, Hayes JD: Characterization of a human class-Theta glutathione S-transferase with activity towards 1-menaphthyl sulphate. Biochem J. 1992 Sep 15;286 ( Pt 3):929-35. [PubMed Link Image]
  5. Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed Link Image]
  6. Rossjohn J, McKinstry WJ, Oakley AJ, Verger D, Flanagan J, Chelvanayagam G, Tan KL, Board PG, Parker MW: Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure. 1998 Mar 15;6(3):309-22. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6100
Enzyme 17 Name Glutathione S-transferase Mu 4
Enzyme 17 Synonyms
  1. GSTM4-4
  2. GST class-mu 4
  3. GTS-Mu2
Enzyme 17 Gene Name GSTM4
Enzyme 17 Protein Sequence >Glutathione S-transferase Mu 4
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
Enzyme 17 Number of Residues 218
Enzyme 17 Molecular Weight 25562
Enzyme 17 Theoretical pI 5.69
Enzyme 17 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Active on 1- chloro-2,4-dinitrobenzene
Enzyme 17 Pathways
Enzyme 17 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-16
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 306819 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q03013 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name GSTM4_HUMAN Link Image
Enzyme 17 PDB ID 4GTU Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTAGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
Enzyme 17 GenBank Gene ID M96234 Link Image
Enzyme 17 GeneCard ID GSTM4 Link Image
Enzyme 17 GenAtlas ID GSTM4 Link Image
Enzyme 17 HGNC ID HGNC:4636 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1p13.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Comstock KE, Johnson KJ, Rifenbery D, Henner WD: Isolation and analysis of the gene and cDNA for a human Mu class glutathione S-transferase, GSTM4. J Biol Chem. 1993 Aug 15;268(23):16958-65. [PubMed Link Image]
  2. Zhong S, Spurr NK, Hayes JD, Wolf CR: Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4. Biochem J. 1993 Apr 1;291 ( Pt 1):41-50. [PubMed Link Image]
  3. Ross VL, Board PG: Molecular cloning and heterologous expression of an alternatively spliced human Mu class glutathione S-transferase transcript. Biochem J. 1993 Sep 1;294 ( Pt 2):373-80. [PubMed Link Image]
  4. Taylor JB, Oliver J, Sherrington R, Pemble SE: Structure of human glutathione S-transferase class Mu genes. Biochem J. 1991 Mar 1;274 ( Pt 2):587-93. [PubMed Link Image]
  5. Comstock KE, Widersten M, Hao XY, Henner WD, Mannervik B: A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes. Arch Biochem Biophys. 1994 Jun;311(2):487-95. [PubMed Link Image]
  6. Patskovsky YV, Patskovska LN, Listowsky I: An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases. Biochemistry. 1999 Dec 7;38(49):16187-94. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6101
Enzyme 18 Name Glutathione S-transferase Mu 5
Enzyme 18 Synonyms
  1. GSTM5-5
  2. GST class-mu 5
Enzyme 18 Gene Name GSTM5
Enzyme 18 Protein Sequence >Glutathione S-transferase Mu 5
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLN
LKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
Enzyme 18 Number of Residues 218
Enzyme 18 Molecular Weight 25675
Enzyme 18 Theoretical pI 7.49
Enzyme 18 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 18 Pathways
Enzyme 18 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-16
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 468260 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P46439 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name GSTM5_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >657 bp
ATGCCCATGACTCTGGGGTACTGGGACATCCGTGGGCTGGCCCACGCCATCCGCTTGCTC
CTGGAATACACAGACTCAAGCTATGTGGAAAAGAAGTACACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAATGCCATCCTGCGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGTTATGGATAACCACATGGAGCTGGTCAGACTGTGCTATGACCCAGATTTT
GAGAAACTGAAGCCAAAATACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAGACAAGATCACCTTTGTGGATTTCCTTGCC
TATGATGTCCTTGACATGAAGCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCTAAAC
TTGAAGGACTTCATCTCCCGCTTTGAGGGTTTGAAGAAGATCTCTGCCTACATGAAGTCC
AGCCAATTCCTCCGAGGTCTTTTGTTTGGAAAGTCAGCTACATGGAACAGCAAATAG
Enzyme 18 GenBank Gene ID L02321 Link Image
Enzyme 18 GeneCard ID GSTM5 Link Image
Enzyme 18 GenAtlas ID GSTM5 Link Image
Enzyme 18 HGNC ID HGNC:4637 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p13.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Takahashi Y, Campbell EA, Hirata Y, Takayama T, Listowsky I: A basis for differentiating among the multiple human Mu-glutathione S-transferases and molecular cloning of brain GSTM5. J Biol Chem. 1993 Apr 25;268(12):8893-8. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6102
Enzyme 19 Name Microsomal glutathione S-transferase 2
Enzyme 19 Synonyms
  1. Microsomal GST- 2
  2. Microsomal GST-II
Enzyme 19 Gene Name MGST2
Enzyme 19 Protein Sequence >Microsomal glutathione S-transferase 2
MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFY
PIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTL
LGALGIANSFLDEYLDLNIAKKLRRQF
Enzyme 19 Number of Residues 147
Enzyme 19 Molecular Weight 16621
Enzyme 19 Theoretical pI 9.88
Enzyme 19 GO Classification
Function
  • enzyme activator activity
  • enzyme regulator activity
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid metabolism
  • icosanoid metabolism
  • leukotriene metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Can catalyze the production of LTC4 from LTA4 and reduced glutathione. Can catalyze the conjugation of 1-chloro-2,4- dinitrobenzene with reduced glutathione
Enzyme 19 Pathways
Enzyme 19 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-23
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 1747521 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q99735 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name MGST2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >444 bp
ATGGCCGGGAACTCGATCCTGCTGGCTGCTGTCTCTATTCTCTCGGCCTGTCAGCAAAGT
TATTTTGCTTTGCAAGTTGGAAAGGCAAGATTAAAATACAAAGTTACGCCCCCAGCAGTC
ACTGGGTCACCAGAGTTTGAGAGAGTATTTCGGGCACAACAAAACTGTGTGGAGTTTTAT
CCTATATTCATAATTACATTGTGGATGGCTGGGTGGTATTTCAACCAAGTTTTTGCTACT
TGTCTGGGTCTGGTGTACATATATGGCCGTCACCTATACTTCTGGGGATATTCAGAAGCT
GCTAAAAAACGGATCACCGGTTTCCGACTGAGTCTGGGGATTTTGGCCTTGTTGACCCTC
CTAGGTGCCCTGGGAATTGCAAACAGCTTTCTGGATGAATATCTGGACCTCAATATTGCC
AAGAAACTGAGGCGGCAATTCTAA
Enzyme 19 GenBank Gene ID U77604 Link Image
Enzyme 19 GeneCard ID MGST2 Link Image
Enzyme 19 GenAtlas ID MGST2 Link Image
Enzyme 19 HGNC ID HGNC:7063 Link Image
Enzyme 19 Chromosome Location 4
Enzyme 19 Locus 4q28.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Jakobsson PJ, Mancini JA, Ford-Hutchinson AW: Identification and characterization of a novel human microsomal glutathione S-transferase with leukotriene C4 synthase activity and significant sequence identity to 5-lipoxygenase-activating protein and leukotriene C4 synthase. J Biol Chem. 1996 Sep 6;271(36):22203-10. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6103
Enzyme 20 Name Glutathione transferase omega-1
Enzyme 20 Synonyms
  1. GSTO 1-1
Enzyme 20 Gene Name GSTO1
Enzyme 20 Protein Sequence >Glutathione transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
Enzyme 20 Number of Residues 241
Enzyme 20 Molecular Weight 27566
Enzyme 20 Theoretical pI 6.54
Enzyme 20 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 20 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 20 Specific Function Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities
Enzyme 20 Pathways
Enzyme 20 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 2393722 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P78417 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name GSTO1_HUMAN Link Image
Enzyme 20 PDB ID 1EEM Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >726 bp
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA
Enzyme 20 GenBank Gene ID U90313 Link Image
Enzyme 20 GeneCard ID GSTO1 Link Image
Enzyme 20 GenAtlas ID GSTO1 Link Image
Enzyme 20 HGNC ID HGNC:13312 Link Image
Enzyme 20 Chromosome Location 10
Enzyme 20 Locus 10q25.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J: Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem. 2000 Aug 11;275(32):24798-806. [PubMed Link Image]
  2. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed Link Image]
  3. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed Link Image]
  4. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6104
Enzyme 21 Name Glutathione S-transferase A5
Enzyme 21 Synonyms
  1. Glutathione S-transferase A5-5
  2. GST class-alpha member 5
Enzyme 21 Gene Name GSTA5
Enzyme 21 Protein Sequence >Glutathione S-transferase A5
MAEKPKLHYSNARGSMESIRWLLAAAGVELEEKFLESAEDLDKLRNDGSLLFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDMKERALIDMYTEGIVDLTEMILLLLICQPEERDAK
TALVKEKIKNRYFPAFEKVLKSHRQDYLVGNKLSWADIHLVELFYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSQRKPPMDEKSLEEARKIFRF
Enzyme 21 Number of Residues 222
Enzyme 21 Molecular Weight 25722
Enzyme 21 Theoretical pI 8.37
Enzyme 21 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function RX + glutathione = HX + R-S-glutathione
Enzyme 21 Pathways
Enzyme 21 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 23197582 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q7RTV2 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name GSTA5_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATGCACGGGGCAGTATGGAGTCCATTCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTGGAAGAGAAATTTCTAGAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGGAGTTTGCTGTTCCAGCAAGTACCAATGGTTGAGATT
GACGGGATGAAGCTGGTGCAGACCAGAGCCATTCTTAACTACATTGCCAGCAAATACAAC
CTTTATGGGAAAGACATGAAGGAGAGAGCCCTGATTGATATGTACACAGAAGGTATAGTA
GATTTGACTGAAATGATCCTTCTTCTGCTCATATGTCAACCAGAGGAAAGAGATGCCAAG
ACTGCCTTGGTCAAAGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACAGACAAGACTACCTTGTTGGCAACAAGCTGAGCTGGGCTGACATTCACCTG
GTGGAACTTTTCTACTACGTGGAAGAGCTTGACTCGAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTGCAGCCT
GGCAGCCAGAGAAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 21 GenBank Gene ID BK000212 Link Image
Enzyme 21 GeneCard ID GSTA5 Link Image
Enzyme 21 GenAtlas ID GSTA5 Link Image
Enzyme 21 HGNC ID HGNC:19662 Link Image
Enzyme 21 Chromosome Location 6
Enzyme 21 Locus 6p12.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Morel F, Rauch C, Coles B, Le Ferrec E, Guillouzo A: The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter. Pharmacogenetics. 2002 Jun;12(4):277-86. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6105
Enzyme 22 Name Glutathione S-transferase A2
Enzyme 22 Synonyms
  1. GTH2
  2. HA subunit 2
  3. GST- gamma
  4. GSTA2-2
  5. GST class-alpha member 2
Enzyme 22 Gene Name GSTA2
Enzyme 22 Protein Sequence >Glutathione S-transferase A2
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
Enzyme 22 Number of Residues 222
Enzyme 22 Molecular Weight 25664
Enzyme 22 Theoretical pI 9.07
Enzyme 22 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 22 Pathways
Enzyme 22 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 306811 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P09210 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name GSTA2_HUMAN Link Image
Enzyme 22 PDB ID 1AGS Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 22 GenBank Gene ID M16594 Link Image
Enzyme 22 GeneCard ID GSTA2 Link Image
Enzyme 22 GenAtlas ID GSTA2 Link Image
Enzyme 22 HGNC ID HGNC:4627 Link Image
Enzyme 22 Chromosome Location 6
Enzyme 22 Locus 6p12.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Rhoads DM, Zarlengo RP, Tu CP: The basic glutathione S-transferases from human livers are products of separate genes. Biochem Biophys Res Commun. 1987 May 29;145(1):474-81. [PubMed Link Image]
  2. Rohrdanz E, Nguyen T, Pickett CB: Isolation and characterization of the human glutathione S-transferase A2 subunit gene. Arch Biochem Biophys. 1992 Nov 1;298(2):747-52. [PubMed Link Image]
  3. Klone A, Hussnatter R, Sies H: Cloning, sequencing and characterization of the human alpha glutathione S-transferase gene corresponding to the cDNA clone pGTH2. Biochem J. 1992 Aug 1;285 ( Pt 3):925-8. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Ahmad H, Singhal SS, Saxena M, Awasthi YC: Characterization of two novel subunits of the alpha-class glutathione S-transferases of human liver. Biochim Biophys Acta. 1993 Feb 13;1161(2-3):333-6. [PubMed Link Image]
  6. Hayes JD, Kerr LA, Cronshaw AD: Evidence that glutathione S-transferases B1B1 and B2B2 are the products of separate genes and that their expression in human liver is subject to inter-individual variation. Molecular relationships between the B1 and B2 subunits and other Alpha class glutathione S-transferases. Biochem J. 1989 Dec 1;264(2):437-45. [PubMed Link Image]
  7. Tetlow N, Liu D, Board P: Polymorphism of human Alpha class glutathione transferases. Pharmacogenetics. 2001 Oct;11(7):609-17. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6106
Enzyme 23 Name Glutathione peroxidase 6 precursor
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name GPX6
Enzyme 23 Protein Sequence >Glutathione peroxidase 6 precursor
MFQQFQASCLVLFFLVGFAQQTLKPQNRKVDCNKGVTGTIYEYGALTLNGEEYIQFKQFA
GKHVLFVNVAAYCGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGLK
YVCPGSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSSSQLFWEPMKVHDIR
WNFEKFLVGPDGVPVMHWFHQAPVSTVKSDILEYLKQFNTH
Enzyme 23 Number of Residues 221
Enzyme 23 Molecular Weight 24924
Enzyme 23 Theoretical pI 6.66
Enzyme 23 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 23 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 23 Specific Function 2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O
Enzyme 23 Pathways
Enzyme 23 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-19
Enzyme 23 Transmembrane Regions Not Available
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 32492913 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P59796 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name GPX6_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >666 bp
ATGTTCCAGCAGTTCCAGGCCTCCTGTCTTGTCCTGTTTTTCCTGGTTGGCTTTGCTCAG
CAGACCCTAAAGCCTCAAAATAGGAAGGTGGATTGCAACAAAGGGGTAACAGGCACCATC
TATGAGTATGGAGCCCTCACCCTCAACGGCGAGGAGTACATCCAATTCAAGCAGTTTGCA
GGCAAGCACGTCCTGTTTGTCAATGTGGCCGCCTATTGAGGCTTGGCAGCTCAGTATCCT
GAACTGAATGCACTACAGGAGGAGCTGAAGAATTTTGGTGTCATTGTGTTGGCCTTTCCC
TGCAACCAGTTTGGAAAACAAGAACCAGGAACAAACTCAGAAATACTTCTTGGTCTCAAG
TATGTGTGTCCAGGTAGTGGCTTTGTCCCCAGTTTCCAGCTCTTTGAGAAAGGGGATGTG
AATGGAGAAAAAGAACAGAAGGTCTTTACTTTCCTGAAGAACTCCTGCCCTCCGACCTCT
GATCTTTTGGGCTCATCAAGCCAACTCTTCTGGGAGCCCATGAAGGTCCATGATATCCGC
TGGAACTTTGAGAAATTTCTGGTGGGGCCCGATGGAGTCCCTGTCATGCATTGGTTCCAC
CAGGCTCCAGTCAGCACAGTCAAGTCAGACATCCTGGAGTACCTAAAGCAGTTCAATACC
CACTAG
Enzyme 23 GenBank Gene ID AY324826 Link Image
Enzyme 23 GeneCard ID GPX6 Link Image
Enzyme 23 GenAtlas ID GPX6 Link Image
Enzyme 23 HGNC ID HGNC:4558 Link Image
Enzyme 23 Chromosome Location 6
Enzyme 23 Locus 6p22.1
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6107
Enzyme 24 Name Glutathione S-transferase A3
Enzyme 24 Synonyms
  1. Glutathione S-transferase A3-3
  2. GST class-alpha member 3
Enzyme 24 Gene Name GSTA3
Enzyme 24 Protein Sequence >Glutathione S-transferase A3
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
Enzyme 24 Number of Residues 222
Enzyme 24 Molecular Weight 25302
Enzyme 24 Theoretical pI 9.69
Enzyme 24 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively
Enzyme 24 Pathways
Enzyme 24 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 951352 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q16772 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name GSTA3_HUMAN Link Image
Enzyme 24 PDB ID 1TDI Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >688 bp
AAACCAGAAGACTGTTACCATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGG
CAGAATGGAGCCCATCCGGTGGCTCTTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATT
TATAGGATCTGCAGAAGATTTGGGAAAGTTAAGAAATGATGGAAGTTTGATGTTCCAGCA
AGTGCCAATGGTTGAGATTGATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTA
CATTGCCAGCAAATACAACCTCTATGGGAAAGACATAAAGGAGAGAGCCCTAATTGATAT
GTATACAGAAGGTATGGCAGATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCCAGC
TGAGGAAAAAGATGCCAAGATTGCCTTGATCAAAGAGAAAATAAAAAGTCGCTATTTCCC
TGCCTTCGAAAAAGTGTTACAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAG
CCGGGCTGACATTAGCCTGGTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCT
TATCTCCAACTTCCCTCTGCTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGT
GAAGAAGTTTCTACAGCCTGGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGA
AGAAGCCAGAAAGATTTTCAGGTTTTAA
Enzyme 24 GenBank Gene ID L13275 Link Image
Enzyme 24 GeneCard ID GSTA3 Link Image
Enzyme 24 GenAtlas ID GSTA3 Link Image
Enzyme 24 HGNC ID HGNC:4628 Link Image
Enzyme 24 Chromosome Location 6
Enzyme 24 Locus 6p12.1
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Suzuki T, Johnston PN, Board PG: Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. Genomics. 1993 Dec;18(3):680-6. [PubMed Link Image]
  2. Johansson AS, Mannervik B: Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J Biol Chem. 2001 Aug 31;276(35):33061-5. Epub 2001 Jun 20. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Board PG: Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochem J. 1998 Mar 1;330 ( Pt 2):827-31. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6108
Enzyme 25 Name Glutathione S-transferase A4
Enzyme 25 Synonyms
  1. Glutathione S-transferase A4-4
  2. GST class-alpha member 4
Enzyme 25 Gene Name GSTA4
Enzyme 25 Protein Sequence >Glutathione S-transferase A4
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
Enzyme 25 Number of Residues 222
Enzyme 25 Molecular Weight 25705
Enzyme 25 Theoretical pI 8.72
Enzyme 25 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4- hydroxynonenal (4-HNE)
Enzyme 25 Pathways
Enzyme 25 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 2597924 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O15217 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name GSTA4_HUMAN Link Image
Enzyme 25 PDB ID 1GUM Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >669 bp
ATGGCAGCAAGGCCCAAGCTCCACTATCCCAACGGAAGAGGCCGGATGGAGTCCGTGAGA
TGGGTTTTAGCTGCCGCCGGAGTCGAGTTTGATGAAGAATTTCTGGAAACAAAAGAACAG
TTGTACAAGTTGCAGGATGGTAACCACCTGCTGTTCCAACAAGTGCCCATGGTTGAAATT
GACGGGATGAAGTTGGTACAGACCCGAAGCATTCTCCACTACATAGCAGACAAGCACAAT
CTCTTTGGCAAGAACCTCAAGGAGAGAACCCTGATTGACATGTACGTGGAGGGGACACTG
GATCTGCTGGAACTGCTTATCATGCATCCTTTCTTAAAACCAGATGATCAGCAAAAGGAA
GTGGTTAACATGGCCCAGAAGGCTATAATTAGATACTTTCCTGTGTTTGAAAAGATTTTA
AGGGGTCACGGACAAAGCTTTCTTGTTGGTAATCAGCTGAGCCTTGCAGATGTGATTTTA
CTCCAAACCATTTTAGCTCTAGAAGAGAAAATTCCTAATATCCTGTCTGCATTTCCTTTC
CTCCAGGAATACACAGTGAAACTAAGTAATATCCCTACAATTAAGAGATTCCTTGAACCT
GGCAGCAAGAAGAAGCCTCCCCCTGATGAAATTTATGTGAGAACCGTCTACAACATCTTT
AGGCCATAA
Enzyme 25 GenBank Gene ID Y13047 Link Image
Enzyme 25 GeneCard ID GSTA4 Link Image
Enzyme 25 GenAtlas ID GSTA4 Link Image
Enzyme 25 HGNC ID HGNC:4629 Link Image
Enzyme 25 Chromosome Location 6
Enzyme 25 Locus 6p12.1
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Hubatsch I, Ridderstrom M, Mannervik B: Human glutathione transferase A4-4: an alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem J. 1998 Feb 15;330 ( Pt 1):175-9. [PubMed Link Image]
  2. Board PG: Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochem J. 1998 Mar 1;330 ( Pt 2):827-31. [PubMed Link Image]
  3. Liu S, Stoesz SP, Pickett CB: Identification of a novel human glutathione S-transferase using bioinformatics. Arch Biochem Biophys. 1998 Apr 15;352(2):306-13. [PubMed Link Image]
  4. Desmots F, Rauch C, Henry C, Guillouzo A, Morel F: Genomic organization, 5'-flanking region and chromosomal localization of the human glutathione transferase A4 gene. Biochem J. 1998 Dec 1;336 ( Pt 2):437-42. [PubMed Link Image]
  5. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  6. Bruns CM, Hubatsch I, Ridderstrom M, Mannervik B, Tainer JA: Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J Mol Biol. 1999 May 7;288(3):427-39. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6109
Enzyme 26 Name Glutathione peroxidase 1
Enzyme 26 Synonyms
  1. GSHPx-1
  2. GPx-1
  3. Cellular glutathione peroxidase
Enzyme 26 Gene Name GPX1
Enzyme 26 Protein Sequence >Glutathione peroxidase 1
MCAARLAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLCGTTVRDYTQMNEL
QRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGA
HPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRR
FQTIDIEPDIEALLSQGPSCA
Enzyme 26 Number of Residues 201
Enzyme 26 Molecular Weight 21899
Enzyme 26 Theoretical pI 6.50
Enzyme 26 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 26 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 26 Specific Function Protects the hemoglobin in erythrocytes from oxidative breakdown
Enzyme 26 Pathways
Enzyme 26 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-16
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 577777 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P07203 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name GPX1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >606 bp
ATGTGTGCTGCTCGGCTAGCGGCGGCGGCGGCCCAGTCGGTGTATGCCTTCTCGGCGCGC
CCGTTGGCCGGCGGGGAGCCTGTGAGCCTGGGCTCCCTGCGGGGCAAGGTACTACTTATC
GAGAATGTGGCGTCCCTCTGAGGCACCACGGTCCGGGACTACACCCAGATGAACGAGCTG
CAGCGGCGCCTCGGACCCCGGGGCCTGGTGGTGCTCGGCTTCCCGTGCAACCAGTTTGGG
CATCAGGAGAACGCCAAGAACGAAGAGATTCTGAATTCCCTCAAGTACGTCCGGCCTGGT
GGTGGGTTCGAGCCCAACTTCATGCTCTTCGAGAAGTGCGAGGTGAACGGTGCGGGGGCG
CACCCTCTCTTCGCCTTCCTGCGGGAGGCCCTGCCAGCTCCCAGCGACGACGCCACCGCG
CTTATGACCGACCCCAAGCTCATCACCTGGTCTCCGGTGTGTCGCAACGATGTTGCCTGG
AACTTTGAGAAGTTCCTGGTGGGCCCTGACGGTGTGCCCCTACGCAGGTACAGCCGCCGC
TTCCAGACCATTGACATCGAGCCTGACATCGAAGCCCTGCTGTCTCAAGGGCCCAGCTGT
GCCTAG
Enzyme 26 GenBank Gene ID Y00433 Link Image
Enzyme 26 GeneCard ID GPX1 Link Image
Enzyme 26 GenAtlas ID GPX1 Link Image
Enzyme 26 HGNC ID HGNC:4553 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3p21.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Sukenaga Y, Ishida K, Takeda T, Takagi K: cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178. [PubMed Link Image]
  2. Ishida K, Morino T, Takagi K, Sukenaga Y: Nucleotide sequence of a human gene for glutathione peroxidase. Nucleic Acids Res. 1987 Dec 10;15(23):10051. [PubMed Link Image]
  3. Mullenbach GT, Tabrizi A, Irvine BD, Bell GI, Hallewell RA: Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 1987 Jul 10;15(13):5484. [PubMed Link Image]
  4. Chada S, Le Beau MM, Casey L, Newburger PE: Isolation and chromosomal localization of the human glutathione peroxidase gene. Genomics. 1990 Feb;6(2):268-71. [PubMed Link Image]
  5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed Link Image]
  6. Forsberg L, de Faire U, Morgenstern R: Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1. Hum Mutat. 1999;13(4):294-300. [PubMed Link Image]
  7. Kote-Jarai Z, Durocher F, Edwards SM, Hamoudi R, Jackson RA, Ardern-Jones A, Murkin A, Dearnaley DP, Kirby R, Houlston R, Easton DF, Eeles R: Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer. Prostate Cancer Prostatic Dis. 2002;5(3):189-92. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6110
Enzyme 27 Name Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
Enzyme 27 Synonyms
  1. PHGPx
  2. GPX-4
Enzyme 27 Gene Name GPX4
Enzyme 27 Protein Sequence >Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
MSLGRLCRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVNLDKYR
GFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFA
AGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKRY
GPMEEPLVIEKDLPHYF
Enzyme 27 Number of Residues 197
Enzyme 27 Molecular Weight 22128
Enzyme 27 Theoretical pI 8.41
Enzyme 27 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 27 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 27 Specific Function Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage
Enzyme 27 Pathways
Enzyme 27 Reactions
  • 2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-25
Enzyme 27 Transmembrane Regions Not Available
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 825667 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P36969 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name GPX4_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >594 bp
ATGAGCCTCGGCCGCCTTTGCCGCCTACTGAAGCCGGCGCTGCTCTGTGGGGCTCTGGCC
GCGCCTGGCCTGGCCGGGACCATGTGCGCGTCCCGGGACGACTGGCGCTGTGCGCGCTCC
ATGCACGAGTTTTCCGCCAAGGACATCGACGGGCACATGGTTAACCTGGACAAGTACCGG
GGCTTCGTGTGCATCGTCACCAACGTGGCCTCCCAGTGAGGCAAGACCGAAGTAAACTAC
ACTCAGCTCGTCGACCTGCACGCCCGATACGCTGAGTGTGGTTTGCGGATCCTGGCCTTC
CCGTGTAACCAGTTCGGGAAGCAGGAGCCAGGGAGTAACGAAGAGATCAAAGAGTTCGCC
GCGGGCTACAACGTCAAATTCGATATGTTCAGCAAGATCTGCGTGAACGGGGACGACGCC
CACCCGCTGTGGAAGTGGATGAAGATCCAACCCAAGGGCAAGGGCATCCTGGGAAATGCC
ATCAAGTGGAACTTCACCAAGTTCCTCATCGACAAGAACGGCTGCGTGGTGAAGCGCTAC
GGACCCATGGAGGAGCCCCTGGTGATAGAGAAGGACCTGCCCCACTATTTCTAG
Enzyme 27 GenBank Gene ID X71973 Link Image
Enzyme 27 GeneCard ID GPX4 Link Image
Enzyme 27 GenAtlas ID GPX4 Link Image
Enzyme 27 HGNC ID HGNC:4556 Link Image
Enzyme 27 Chromosome Location 19
Enzyme 27 Locus 19p13.3
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Esworthy RS, Doan K, Doroshow JH, Chu FF: Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene. 1994 Jul 8;144(2):317-8. [PubMed Link Image]
  2. Kelner MJ, Montoya MA: Structural organization of the human selenium-dependent phospholipid hydroperoxide glutathione peroxidase gene (GPX4): chromosomal localization to 19p13.3. Biochem Biophys Res Commun. 1998 Aug 10;249(1):53-5. [PubMed Link Image]
  3. Maiorino M, Bosello V, Ursini F, Foresta C, Garolla A, Scapin M, Sztajer H, Flohe L: Genetic variations of gpx-4 and male infertility in humans. Biol Reprod. 2003 Apr;68(4):1134-41. Epub 2002 Nov 27. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6111
Enzyme 28 Name Glutathione peroxidase 3 precursor
Enzyme 28 Synonyms
  1. GSHPx-3
  2. GPx-3
  3. Plasma glutathione peroxidase
  4. GSHPx-P
  5. Extracellular glutathione peroxidase
  6. GPx-P
Enzyme 28 Gene Name GPX3
Enzyme 28 Protein Sequence >Glutathione peroxidase 3 precursor
MARLLQASCLLSLLLAGFVSQSRGQEKSKMDCHGGISGTIYEYGALTIDGEEYIPFKQYA
GKYVLFVNVASYCGLTGQYIELNALQEELAPFGLVILGFPCNQFGKQEPGENSEILPTLK
YVRPGGGFVPNFQLFEKGDVNGEKEQKFYTFLKNSCPPTSELLGTSDRLFWEPMKVHDIR
WNFEKFLVGPDGIPIMRWHHRTTVSNVKMDILSYMRRQAALGVKRK
Enzyme 28 Number of Residues 226
Enzyme 28 Molecular Weight 25506
Enzyme 28 Theoretical pI 8.19
Enzyme 28 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 28 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 28 Specific Function Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione
Enzyme 28 Pathways
Enzyme 28 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-20
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 2160390 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P22352 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name GPX3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >681 bp
ATGGCCCGGCTGCTGCAGGCGTCCTGCCTGCTTTCCCTGCTCCTGGCCGGCTTCGTCTCG
CAGAGCCGGGGACAAGAGAAGTCGAAGATGGACTGCCATGGTGGCATAAGTGGCACCATT
TACGAGTACGGAGCCCTCACCATTGATGGGGAGGAGTACATCCCCTTCAAGCAGTATGCT
GGCAAATACGTCCTCTTTGTCAACGTGGCCAGCTACTGAGGCCTGACGGGCCAGTACATT
GAACTGAATGCACTACAGGAAGAGCTTGCACCATTCGGTCTGGTCATTCTGGGCTTTCCC
TGCAACCAATTTGGAAAACAGGAACCAGGAGAGAACTCAGAGATCCTTCCTACCCTCAAG
TATGTCCGACCAGGTGGAGGCTTTGTCCCTAATTTCCAGCTCTTTGAGAAAGGGGATGTC
AATGGAGAGAAAGAGCAGAAATTCTACACTTTCCTAAAGAACTCCTGTCCTCCCACCTCG
GAGCTCCTGGGTACATCTGACCGCCTCTTCTGGGAACCCATGAAGGTTCACGACATCCGC
TGGAACTTTGAGAAGTTCCTGGTGGGGCCAGATGGTATACCCATCATGCGCTGGCACCAC
CGGACCACGGTCAGCAACGTCAAGATGGACATCCTGTCCTACATGAGGCGGCAGGCAGCC
CTGGGGGTCAAGAGGAAGTAA
Enzyme 28 GenBank Gene ID D00632 Link Image
Enzyme 28 GeneCard ID GPX3 Link Image
Enzyme 28 GenAtlas ID GPX3 Link Image
Enzyme 28 HGNC ID HGNC:4555 Link Image
Enzyme 28 Chromosome Location 5
Enzyme 28 Locus 5q23
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Takahashi K, Akasaka M, Yamamoto Y, Kobayashi C, Mizoguchi J, Koyama J: Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J Biochem (Tokyo). 1990 Aug;108(2):145-8. [PubMed Link Image]
  2. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF: Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents. Blood. 1992 Jun 15;79(12):3233-8. [PubMed Link Image]
  3. Yoshimura S, Suemizu H, Taniguchi Y, Arimori K, Kawabe N, Moriuchi T: The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32. Gene. 1994 Aug 5;145(2):293-7. [PubMed Link Image]
  4. Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol. 2000 Sep;23(3):350-4. [PubMed Link Image]
  5. Esworthy RS, Chu FF, Paxton RJ, Akman S, Doroshow JH: Characterization and partial amino acid sequence of human plasma glutathione peroxidase. Arch Biochem Biophys. 1991 May 1;286(2):330-6. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6112
Enzyme 29 Name Glutathione transferase omega-2
Enzyme 29 Synonyms
  1. GSTO-2
Enzyme 29 Gene Name GSTO2
Enzyme 29 Protein Sequence >Glutathione transferase omega-2
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKP
EWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELF
CKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWP
WFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDF
GLC
Enzyme 29 Number of Residues 243
Enzyme 29 Molecular Weight 28254
Enzyme 29 Theoretical pI 7.62
Enzyme 29 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 29 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 29 Specific Function RX + glutathione = HX + R-S-glutathione
Enzyme 29 Pathways
Enzyme 29 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 37777744 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9H4Y5 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name GSTO2_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >732 bp
ATGTCTGGGGATGCGACCAGGACCCTGGGGAAAGGAAGCCAGCCCCCAGGGCCAGTCCCG
GAGGGGCTGATCCGCATCTACAGCATGAGGTTCTGCCCCTATTCTCACAGGACCCGCCTC
GTCCTCAAGGCCAAAGACATCAGACATGAAGTGGTCAACATTAACCTGAGAAACAAGCCT
GAATGGTACTATACAAAGCACCCTTTTGGCCACATTCCTGTCCTGGAGACCAGCCAATGT
CAACTGATCTATGAATCTGTTATTGCTTGTGAGTACCTGGATGATGCTTATCCAGGAAGG
AAGCTGTTTCCATATGACCCTTATGAACGAGCTCGCCAAAAGATGTTATTGGAGCTATTT
TGTAAGGTCCCACATTTGACCAAGGAGTGCCTGGTAGCGTTGAGATGTGGGAGAGAATGC
ACTAATCTGAAGGCAGCCCTGCGTCAGGAATTCAGCAACCTGGAAGAGATTCTTGAGTAT
CAGAACACCACCTTCTTTGGTGGAACCTGTATATCCATGATTGATTACCTCCTCTGGCCC
TGGTTTGAGCGGCTGGATGTGTATGGGATACTGGACTGTGTGAGCCACACGCCAGCCCTG
CGGCTCTGGATATCAGCCATGAAGTGGGACCCCACAGTCTGTGCTCTTCTCATGGATAAG
AGCATTTTCCAGGGCTTCTTGAATCTCTATTTTCAGAACAACCCTAATGCCTTTGACTTT
GGGCTGTGCTGA
Enzyme 29 GenBank Gene ID AY350731 Link Image
Enzyme 29 GeneCard ID GSTO2 Link Image
Enzyme 29 GenAtlas ID GSTO2 Link Image
Enzyme 29 HGNC ID HGNC:23064 Link Image
Enzyme 29 Chromosome Location 10
Enzyme 29 Locus 10q25.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6113
Enzyme 30 Name Glutathione S-transferase theta-1
Enzyme 30 Synonyms
  1. GST class-theta-1
  2. Glutathione transferase T1-1
Enzyme 30 Gene Name GSTT1
Enzyme 30 Protein Sequence >Glutathione S-transferase theta-1
MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDG
DFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMF
PVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGA
GCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
Enzyme 30 Number of Residues 240
Enzyme 30 Molecular Weight 27335
Enzyme 30 Theoretical pI 7.60
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 30 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2- epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4- nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide
Enzyme 30 Pathways
Enzyme 30 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-16
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 510905 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P30711 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name GSTT1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >723 bp
ATGGGTCTGGAGCTCTACCTGGACCTGCTGTCCCAGCCCTGCCGCGCTGTTTACATCTTT
GCCAAGAAGAACGACATTCCCTTCGAGCTGCGCATCGTGGATCTGATTAAAGGTCAGCAC
TTAAGCGATGCCTTTGCCCAGGTGAACCCCCTCAAGAAGGTGCCGGCCTTGAAGGACGGG
GACTTCACCTTGACGGAGAGTGTGGCCATCCTGCTCTACCTGACGCGCAAATATAAGGTC
CCTGACTACTGGTACCCTCAGGACCTGCAGGCCCGTGCCCGTGTGGATGAGTACCTGGCA
TGGCAGCACACGACTCTGCGGAGAAGCTGCCTCCGGGCCTTGTGGCATAAGGTGATGTTC
CCTGTGTTCCTGGGTGGGCCAGTATCTCCCCAGACACTGGCAGCCACCCTGGCAGAGTTG
GATGTGACCCTGCAGTTGCTCGAGGACAAGTTCCTCCAGAACAAGGCCTTCCTTACTGGT
CCTCACATCTCCTTAGCTGACCTCGTAGCCATCACGGAGCTGATGCATCCCGTGGGTGCT
GGCTGCCAAGTCTTCGAAGGCCGACCCAAGCTGGCCACATGGCGGCAGCGCGTGGAGGCA
GCAGTGGGGGAGGACCTCTTCCAGGAGGCCCATGAGGTCATTCTGAAGGCCAAGGACTTC
CCACCTGCAGACCCCACCATAAAGCAGAAGCTGATGCCCTGGGTGCTGGCCATGATCCGG
TGA
Enzyme 30 GenBank Gene ID X79389 Link Image
Enzyme 30 GeneCard ID GSTT1 Link Image
Enzyme 30 GenAtlas ID GSTT1 Link Image
Enzyme 30 HGNC ID HGNC:4641 Link Image
Enzyme 30 Chromosome Location 22
Enzyme 30 Locus 22q11.23
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Pemble S, Schroeder KR, Spencer SR, Meyer DJ, Hallier E, Bolt HM, Ketterer B, Taylor JB: Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism. Biochem J. 1994 May 15;300 ( Pt 1):271-6. [PubMed Link Image]
  2. Jemth P, Mannervik B: Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme. Arch Biochem Biophys. 1997 Dec 15;348(2):247-54. [PubMed Link Image]
  3. Sprenger R, Schlagenhaufer R, Kerb R, Bruhn C, Brockmoller J, Roots I, Brinkmann U: Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation. Pharmacogenetics. 2000 Aug;10(6):557-65. [PubMed Link Image]
  4. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  5. Meyer DJ, Coles B, Pemble SE, Gilmore KS, Fraser GM, Ketterer B: Theta, a new class of glutathione transferases purified from rat and man. Biochem J. 1991 Mar 1;274 ( Pt 2):409-14. [PubMed Link Image]
  6. Mainwaring GW, Williams SM, Foster JR, Tugwood J, Green T: The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human. Biochem J. 1996 Aug 15;318 ( Pt 1):297-303. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6114
Enzyme 31 Name Glutathione peroxidase 2
Enzyme 31 Synonyms
  1. GSHPx-2
  2. GPx-2
  3. Glutathione peroxidase-gastrointestinal
  4. GSHPx-GI
  5. Glutathione peroxidase- related protein 2
  6. Gastrointestinal glutathione peroxidase
  7. GPRP
Enzyme 31 Gene Name GPX2
Enzyme 31 Protein Sequence >Glutathione peroxidase 2
MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLCGTTTRDFTQLNELQCRFPRR
LVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLK
DKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEP
DIKRLLKVAI
Enzyme 31 Number of Residues 190
Enzyme 31 Molecular Weight 21907
Enzyme 31 Theoretical pI 7.84
Enzyme 31 GO Classification
Function
  • antioxidant activity
  • glutathione peroxidase activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
Enzyme 31 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 31 Specific Function Could play a major role in protecting mammals from the toxicity of ingested organic hydroperoxides. Tert-butyl hydroperoxide, cumene hydroperoxide and linoleic acid hydroperoxide but not phosphatidycholine hydroperoxide, can act as acceptors
Enzyme 31 Pathways
Enzyme 31 Reactions
  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 4902773 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P18283 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name GPX2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >573 bp
ATGGCTTTCATTGCCAAGTCCTTCTATGACCTCAGTGCCATCAGCCTGGATGGGGAGAAG
GTAGATTTCAATACGTTCCGGGGCAGGGCCGTGCTGATTGAGAATGTGCGTTCGCTCTGA
GGCACAACCACCCGGGACTTCACCCAGCTCAACGAGCTGCAATGCCGCTTTCCCAGGCGC
CTGGTGGTCCTTGGCTTCCCTTGCAACCAATTTGGACATCAGGAGAACAGTCAGAATGAG
GAGATCCTGAACAGTCTCAAGTATGTCCGTCCTGGGGGTGGATACCAGCCCACCTTCACC
CTTGTCCAAAAATGTGAGGTGAATGGGCAGAACGAGCATCCTGTCTTCGCCTACCTGAAG
GACAAGCTCCCCTACCCTTATGATGACCCATTTTCCCTCATGACCGATCCCAAGCTCATC
ATTTGGAGCCCTGTGCGCCGCTCAGATGTGGCCTGGAACTTTGAGAAGTTCCTCATAGGG
CCGGAGGGAGAGCCCTTCCGACGCTACAGCCGCACCTTCCCAACCATCAACATTGAGCCT
GACATCAAGCGCCTCCTTAAAGTTGCCATATAG
Enzyme 31 GenBank Gene ID X53463 Link Image
Enzyme 31 GeneCard ID GPX2 Link Image
Enzyme 31 GenAtlas ID GPX2 Link Image
Enzyme 31 HGNC ID HGNC:4554 Link Image
Enzyme 31 Chromosome Location 14
Enzyme 31 Locus 14q24.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Akasaka M, Mizoguchi J, Takahashi K: A human cDNA sequence of a novel glutathione peroxidase-related protein. Nucleic Acids Res. 1990 Aug 11;18(15):4619. [PubMed Link Image]
  2. Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem. 1993 Feb 5;268(4):2571-6. [PubMed Link Image]
  3. Kelner MJ, Bagnell RD, Montoya MA, Lanham KA: Structural organization of the human gastrointestinal glutathione peroxidase (GPX2) promoter and 3'-nontranscribed region: transcriptional response to exogenous redox agents. Gene. 2000 May 2;248(1-2):109-16. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6115
Enzyme 32 Name Glutathione S-transferase P
Enzyme 32 Synonyms
  1. GST class-pi
  2. GSTP1-1
Enzyme 32 Gene Name GSTP1
Enzyme 32 Protein Sequence >Glutathione S-transferase P
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGD
LTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAY
VGRLSARPKLKAFLASPEYVNLPINGNGKQ
Enzyme 32 Number of Residues 210
Enzyme 32 Molecular Weight 23356
Enzyme 32 Theoretical pI 5.30
Enzyme 32 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 32 Pathways
Enzyme 32 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • 1-17
Enzyme 32 Transmembrane Regions Not Available
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 31946 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P09211 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name GSTP1_HUMAN Link Image
Enzyme 32 PDB ID 13GS Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >633 bp
ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG
CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG
GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC
CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT
GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC
CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG
AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC
AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG
CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT
GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG
AACCTCCCCATCAATGGCAACGGGAAACAGTGA
Enzyme 32 GenBank Gene ID X06547 Link Image
Enzyme 32 GeneCard ID GSTP1 Link Image
Enzyme 32 GenAtlas ID GSTP1 Link Image
Enzyme 32 HGNC ID HGNC:4638 Link Image
Enzyme 32 Chromosome Location 11
Enzyme 32 Locus 11q13
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Kano T, Sakai M, Muramatsu M: Structure and expression of a human class pi glutathione S-transferase messenger RNA. Cancer Res. 1987 Nov 1;47(21):5626-30. [PubMed Link Image]
  2. Cowell IG, Dixon KH, Pemble SE, Ketterer B, Taylor JB: The structure of the human glutathione S-transferase pi gene. Biochem J. 1988 Oct 1;255(1):79-83. [PubMed Link Image]
  3. Morrow CS, Cowan KH, Goldsmith ME: Structure of the human genomic glutathione S-transferase-pi gene. Gene. 1989 Jan 30;75(1):3-11. [PubMed Link Image]
  4. Moscow JA, Fairchild CR, Madden MJ, Ransom DT, Wieand HS, O'Brien EE, Poplack DG, Cossman J, Myers CE, Cowan KH: Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors. Cancer Res. 1989 Mar 15;49(6):1422-8. [PubMed Link Image]
  5. Ali-Osman F, Akande O, Antoun G, Mao JX, Buolamwini J: Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins. J Biol Chem. 1997 Apr 11;272(15):10004-12. [PubMed Link Image]
  6. Alin P, Mannervik B, Jornvall H: Structural evidence for three different types of glutathione transferase in human tissues. FEBS Lett. 1985 Mar 25;182(2):319-22. [PubMed Link Image]
  7. Mannervik B, Alin P, Guthenberg C, Jensson H, Tahir MK, Warholm M, Jornvall H: Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7202-6. [PubMed Link Image]
  8. Singh SV, Ahmad H, Kurosky A, Awasthi YC: Purification and characterization of unique glutathione S-transferases from human muscle. Arch Biochem Biophys. 1988 Jul;264(1):13-22. [PubMed Link Image]
  9. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  10. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed Link Image]
  11. Ahmad H, Wilson DE, Fritz RR, Singh SV, Medh RD, Nagle GT, Awasthi YC, Kurosky A: Primary and secondary structural analyses of glutathione S-transferase pi from human placenta. Arch Biochem Biophys. 1990 May 1;278(2):398-408. [PubMed Link Image]
  12. Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW: Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution. J Mol Biol. 1992 Sep 5;227(1):214-26. [PubMed Link Image]
  13. Oakley AJ, Rossjohn J, Lo Bello M, Caccuri AM, Federici G, Parker MW: The three-dimensional structure of the human Pi class glutathione transferase P1-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry. 1997 Jan 21;36(3):576-85. [PubMed Link Image]
  14. Ji X, Tordova M, O'Donnell R, Parsons JF, Hayden JB, Gilliland GL, Zimniak P: Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochemistry. 1997 Aug 12;36(32):9690-702. [PubMed Link Image]
  15. Oakley AJ, Lo Bello M, Battistoni A, Ricci G, Rossjohn J, Villar HO, Parker MW: The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J Mol Biol. 1997 Nov 21;274(1):84-100. [PubMed Link Image]
  16. Prade L, Huber R, Manoharan TH, Fahl WE, Reuter W: Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor. Structure. 1997 Oct 15;5(10):1287-95. [PubMed Link Image]
  17. Ji X, Blaszczyk J, Xiao B, O'Donnell R, Hu X, Herzog C, Singh SV, Zimniak P: Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1. Biochemistry. 1999 Aug 10;38(32):10231-8. [PubMed Link Image]
  18. Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lo Bello M, Caccuri AM, Federici G, Ricci G: Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure. Biochemistry. 1998 Mar 3;37(9):3020-7. [PubMed Link Image]
  19. Kong KH, Inoue H, Takahashi K: Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1. Protein Eng. 1993 Jan;6(1):93-9. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6871
Enzyme 33 Name Glutathione-requiring prostaglandin D synthase
Enzyme 33 Synonyms
  1. Glutathione-dependent PGD synthetase
  2. Prostaglandin-H2 D-isomerase
  3. Hematopoietic prostaglandin D synthase
  4. H-PGDS
Enzyme 33 Gene Name PTGDS2
Enzyme 33 Protein Sequence >Glutathione-requiring prostaglandin D synthase
MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLT
LHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELL
TYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKK
VQAIPAVANWIKRRPQTKL
Enzyme 33 Number of Residues 199
Enzyme 33 Molecular Weight 23344
Enzyme 33 Theoretical pI 5.64
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation
Enzyme 33 Pathways
Enzyme 33 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 3046817 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID O60760 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PTGD2_HUMAN Link Image
Enzyme 33 PDB ID 1IYI Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >600 bp
ATGCCAAACTACAAACTCACTTATTTTAATATGAGGGGGAGAGCAGAAATTATTCGTTAC
ATATTTGCTTATTTGGACATACAGTATGAAGACCACAGAATAGAACAAGCTGACTGGCCT
GAAATCAAATCAACTCTCCCATTTGGAAAAATCCCCATTTTGGAAGTTGATGGACTTACT
CTTCACCAGAGCCTAGCAATAGCAAGATATTTGACCAAAAACACAGATTTGGCTGGAAAC
ACAGAAATGGAACAATGTCATGTTGATGCTATTGTGGACACTCTGGATGATTTCATGTCA
TGTTTTCCTTGGGCAGAGAAAAAGCAAGATGTGAAAGAGCAGATGTTCAATGAGCTGCTC
ACGTATAATGCGCCTCATCTTATGCAAGACTTGGACACATATTTAGGGGGGAGAGAATGG
CTTATTGGTAACTCTGTAACTTGGGCAGACTTCTACTGGGAGATTTGCAGTACCACACTT
TTGGTCTTTAAGCCTGACCTGTTAGACAACCATCCAAGGCTGGTGACTTTACGGAAGAAA
GTCCAAGCCATTCCTGCCGTCGCTAACTGGATAAAACGAAGGCCCCAAACCAAACTCTAG
Enzyme 33 GenBank Gene ID D82073 Link Image
Enzyme 33 GeneCard ID Not Available
Enzyme 33 GenAtlas ID Not Available
Enzyme 33 HGNC ID Not Available
Enzyme 33 Chromosome Location Not Available
Enzyme 33 Locus Not Available
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Kanaoka Y, Fujimori K, Kikuno R, Sakaguchi Y, Urade Y, Hayaishi O: Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase. Eur J Biochem. 2000 Jun;267(11):3315-22. [PubMed Link Image]
  2. Suzuki T, Watanabe K, Kanaoka Y, Sato T, Hayaishi O: Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester. Biochem Biophys Res Commun. 1997 Dec 18;241(2):288-93. [PubMed Link Image]
  3. Mahmud I, Ueda N, Yamaguchi H, Yamashita R, Yamamoto S, Kanaoka Y, Urade Y, Hayaishi O: Prostaglandin D synthase in human megakaryoblastic cells. J Biol Chem. 1997 Nov 7;272(45):28263-6. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 7832
Enzyme 34 Name RalA-binding protein 1
Enzyme 34 Synonyms
  1. RalBP1
  2. Ral-interacting protein 1
  3. 76 kDa Ral-interacting protein
  4. Dinitrophenyl S-glutathione ATPase
  5. DNP-SG ATPase
Enzyme 34 Gene Name RALBP1
Enzyme 34 Protein Sequence >RalA-binding protein 1
MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDV
VSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKK
KEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQ
IDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKV
DELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKV
QEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVF
FTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGI
KDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVIN
ILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSS
ESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAK
AEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI
Enzyme 34 Number of Residues 655
Enzyme 34 Molecular Weight 76064
Enzyme 34 Theoretical pI 5.68
Enzyme 34 GO Classification Not Available
Enzyme 34 General Function Replication, recombination and repair
Enzyme 34 Specific Function Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDC2 to switch off endocytosis, One of its substrates would be EPN1/Epsin
Enzyme 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 974143 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q15311 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name RBP1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1968 bp
ATGACTGAGTGCTTCCTGCCCCCCACCAGCAGCCCCAGTGAACACCGCAGGGTGGAGCAT
GGCAGCGGGCTTACCCGGACCCCCAGCTCTGAAGAGATCAGCCCTACTAAGTTTCCTGGA
TTGTACCGCACTGGCGAGCCCTCACCTCCCCATGACATCCTCCATGAGCCTCCTGATGTA
GTGTCTGATGATGAGAAAGATCATGGGAAGAAAAAAGGGAAATTTAAGAAAAAGGAAAAG
AGGACTGAAGGCTATGCAGCCTTTCAGGAAGATAGCTCTGGAGATGAGGCAGAAAGTCCT
TCTAAAATGAAGAGGTCCAAGGGAATCCATGTTTTCAAGAAGCCCAGCTTTTCTAAAAAG
AAGGAAAAGGATTTTAAAATAAAAGAGAAACCCAAAGAAGAAAAGCATAAAGAAGAAAAG
CACAAAGAAGAAAAACATAAAGAGAAGAAGTCAAAAGACTTGACAGCAGCTGATGTTGTT
AAACAGTGGAAGGAAAAGAAGAAAAAGAAAAAGCCAATTCAGGAGCCAGAGGTGCCTCAG
ATTGATGTTCCAAATCTCAAACCCATTTTTGGAATTCCTTTGGCTGATGCAGTAGAGAGG
ACCATGATGTATGATGGCATTCGGCTGCCAGCCGTTTTCCGTGAATGTATAGATTACGTA
GAGAAGTATGGCATGAAGTGTGAAGGCATCTACAGAGTATCAGGAATTAAATCAAAGGTG
GATGAGCTAAAAGCAGCCTATGACCGGGAGGAGTCTACAAACTTGGAAGACTATGAGCCT
AACACTGTAGCCAGTTTGCTGAAGCAGTATTTGCGAGACCTTCCAGAGAATTTGCTTACC
AAAGAGCTTATGCCCAGATTTGAAGAGGCTTGTGGGAGGACCACGGAGACTGAGAAAGTG
CAGGAATTCCAGCGTTTACTCAAAGAACTGCCAGAATGTAACTATCTTCTGATTTCTTGG
CTCATTGTGCACATGGACCATGTCATTGCAAAGGAACTGGAAACAAAAATGAATATACAG
AACATTTCTATAGTGCTCAGCCCAACTGTGCAGATCAGCAATCGAGTCCTGTATGTGTTT
TTCACACATGTGCAAGAACTCTTTGGAAATGTGGTACTAAAGCAAGTGATGAAACCTCTG
CGATGGTCTAACATGGCCACGATGCCCACGCTGCCAGAGACCCAGGCGGGCATCAAGGAG
GAGATCAGGAGACAGGAGTTTCTTTTGAATTGTTTACATCGAGATCTGCAGGGTGGGATA
AAGGATTTGTCTAAAGAAGAAAGATTATGGGAAGTACAAAGAATTTTGACAGCCCTCAAA
AGAAAACTGAGAGAAGCTAAAAGACAGGAGTGTGAAACCAAGATTGCACAAGAGATAGCC
AGTCTTTCAAAAGAGGATGTTTCCAAAGAAGAGATGAATGAAAATGAAGAAGTTATAAAT
ATTCTCCTTGCTCAGGAGAATGAGATCCTGACTGAACAGGAGGAGCTCCTGGCCATGGAG
CAGTTTCTGCGCCGGCAGATTGCCTCAGAAAAAGAAGAGATTGAACGCCTCAGAGCTGAG
ATTGCTGAAATTCAGAGTCGCCAGCAGCACGGCCGAAGTGAGACTGAGGAGTACTCCTCC
GAGAGCGAGAGCGAGAGTGAGGATGAGGAGGAGCTGCAGATCATTCTGGAAGACTTACAG
AGACAGAACGAAGAGCTGGAAATAAAGAACAATCATTTGAATCAAGCAATTCATGAGGAG
CGCGAGGCCATCATCGAGCTGCGCGTGCAGCTGCGGCTGCTCCAGATGCAGCGAGCCAAG
GCCGAGCAGCAGGCGCAGGAGGACGAGGAGCCTGAGTGGCGCGGGGGTGCCGTCCAGCCG
CCCAGAGACGGCGTCCTTGAGCCAAAAGCAGCTAAAGAGCAGCCAAAGGCAGGCAAGGAG
CCGGCAAAGCCATCGCCCAGCAGGGATAGGAAGGAGACGTCCATCTGA
Enzyme 34 GenBank Gene ID L42542 Link Image
Enzyme 34 GeneCard ID RALBP1 Link Image
Enzyme 34 GenAtlas ID RALBP1 Link Image
Enzyme 34 HGNC ID HGNC:9841 Link Image
Enzyme 34 Chromosome Location 18
Enzyme 34 Locus 18p11.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH: Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. [PubMed Link Image]
  2. Awasthi S, Cheng J, Singhal SS, Saini MK, Pandya U, Pikula S, Bandorowicz-Pikula J, Singh SV, Zimniak P, Awasthi YC: Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin. Biochemistry. 2000 Aug 8;39(31):9327-34. [PubMed Link Image]
  3. Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A: Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J Biol Chem. 1998 Jan 9;273(2):814-21. [PubMed Link Image]
  4. Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P, Awasthi S, Awasthi YC: RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Arch Biochem Biophys. 2001 Jul 15;391(2):171-9. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 11578
Enzyme 35 Name Hydroxyacylglutathione hydrolase-like protein
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name HAGHL
Enzyme 35 Protein Sequence >Hydroxyacylglutathione hydrolase-like protein
MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHA
RGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLW
EDDCPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLE
FAQKVEPCNDHVRAKLSWAKARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRG
MRMTCPLCRRLWARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG
Enzyme 35 Number of Residues 290
Enzyme 35 Molecular Weight 31558
Enzyme 35 Theoretical pI Not Available
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Not Available
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions
  • H2O + (R)-S-Lactoylglutathione --> Reduced glutathione + H+ + D-Lactate
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 45708670 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q6PII5 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name Q6PII5_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence Not Available
Enzyme 35 GenBank Gene ID BC033796 Link Image
Enzyme 35 GeneCard ID Not Available
Enzyme 35 GenAtlas ID HAGHL Link Image
Enzyme 35 HGNC ID HGNC:14177 Link Image
Enzyme 35 Chromosome Location Not Available
Enzyme 35 Locus Not Available
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 12987
Enzyme 36 Name Gamma-glutamyltransferase 6 homolog
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name GGT6
Enzyme 36 Protein Sequence >Gamma-glutamyltransferase 6 homolog
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWVRV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
Enzyme 36 Number of Residues 493
Enzyme 36 Molecular Weight 50538
Enzyme 36 Theoretical pI 6.04
Enzyme 36 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 36 General Function Amino acid transport and metabolism
Enzyme 36 Specific Function Not Available
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 38970000 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q6P531 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name Q6P531_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence Not Available
Enzyme 36 GenBank Gene ID BC063111 Link Image
Enzyme 36 GeneCard ID Q6P531 Link Image
Enzyme 36 GenAtlas ID GGT6 Link Image
Enzyme 36 HGNC ID HGNC:26891 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 13120
Enzyme 37 Name Uncharacterized protein GSTZ1
Enzyme 37 Synonyms
  1. Glutathione transferase zeta 1
  2. Maleylacetoacetate isomerase, isoform CRA_a
Enzyme 37 Gene Name GSTZ1
Enzyme 37 Protein Sequence >Uncharacterized protein GSTZ1
MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
Enzyme 37 Number of Residues 161
Enzyme 37 Molecular Weight 17896
Enzyme 37 Theoretical pI 5.76
Enzyme 37 GO Classification
Function
  • catalytic activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • aromatic amino acid family metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 37 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 37 Specific Function Not Available
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein Not Available
Enzyme 37 UniProtKB/Swiss-Prot ID A6NNB8 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name A6NNB8_HUMAN Link Image
Enzyme 37 PDB ID 1FW1 Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence Not Available
Enzyme 37 GenBank Gene ID AC007954 Link Image
Enzyme 37 GeneCard ID A6NNB8 Link Image
Enzyme 37 GenAtlas ID GSTZ1 Link Image
Enzyme 37 HGNC ID HGNC:4643 Link Image
Enzyme 37 Chromosome Location Not Available
Enzyme 37 Locus Not Available
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 15189
Enzyme 38 Name GGTL3 protein (Fragment)
Enzyme 38 Synonyms Not Available
Enzyme 38 Gene Name GGTL3
Enzyme 38 Protein Sequence >GGTL3 protein (Fragment)
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLA
Enzyme 38 Number of Residues 592
Enzyme 38 Molecular Weight 62567
Enzyme 38 Theoretical pI 4.64
Enzyme 38 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 38 General Function Amino acid transport and metabolism
Enzyme 38 Specific Function Not Available
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 118600847 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID A0PJJ9 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name A0PJJ9_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1777 bp
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAAGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCC
Enzyme 38 GenBank Gene ID BC033745 Link Image
Enzyme 38 GeneCard ID A0PJJ9 Link Image
Enzyme 38 GenAtlas ID Not Available
Enzyme 38 HGNC ID Not Available
Enzyme 38 Chromosome Location 20
Enzyme 38 Locus 20q11.22
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 15190
Enzyme 39 Name Gamma-glutamyltransferase-like activity 1
Enzyme 39 Synonyms Not Available
Enzyme 39 Gene Name GGTLA1
Enzyme 39 Protein Sequence >Gamma-glutamyltransferase-like activity 1
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAI
LQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPS
LLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVL
SRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRL
GQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLR
GFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQL
IRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRT
GIILNNELLDLCERCPRGSGTTPSPAVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINK
AQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQE
VQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
Enzyme 39 Number of Residues 587
Enzyme 39 Molecular Weight 62333
Enzyme 39 Theoretical pI 7.59
Enzyme 39 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 39 General Function Amino acid transport and metabolism
Enzyme 39 Specific Function Not Available
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 49256405 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q6GMP0 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name Q6GMP0_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1764 bp
ATGGCCCGGGGCTACGGGGCCACGGTCAGCCTAGTCCTGCTGGGTCTGGGGCTGGCGCTG
GCTGTCATTGTGCTGGCTGTGGTCCTCTCTCGACACCAGGCCCCATGTGGCCCCCAGGCC
TTTGCCCACGCTGCTGTTGCCGCCGACTCCAAGGTCTGCTCGGATATTGGACGAGCCATC
CTCCAGCAGCAGGGCTCACCCGTGGATGCCACCATCGCGGCTCTGGTCTGCACCAGCGTC
GTCAACCCTCAGAGCATGGGCCTGGGCGGAGGGGTCATCTTCACCATCTACAATGTGACA
ACAGGGAAGGTGGAGGTCATCAATGCCCGGGAGACGGTGCCGGCCAGCCACGCCCCGAGC
CTGCTGGACCAGTGTGCACAGGCTCTGCCACTGGGCACAGGGGCCCAGTGGATCGGGGTG
CCCGGGGAGCTCCGTGGCTATGCCGAGGCCCACCGCCGCCATGGCCGCCTGCCCTGGGCG
CAGCTGTTCCAGCCCACCATCGCGCTGCTCCGAGGGGGGCATGTGGTGGCCCCTGTCCTC
AGCCGTTTCCTGCACAACAGCATCCTGCGGCCTTCCTTGCAGGCGTCAACCCTGCGCCAG
CTCTTCTTCAACGGGACAGAACCCCTGAGGCCTCAGGACCCACTCCCATGGCCTGCACTG
GCCACCACCCTGGAGACCGTGGCCACAGAGGGCGTGGAGGTCTTCTACACGGGGAGGCTG
GGCCAGATGCTGGTGGAGGACATTGCCAAGGAAGGGAGCCAGCTGACGCTGCAGGACCTG
GCCAAGTTCCAGCCCGAGGTGGTGGATGCCCTGGAGGTGCCCCTGGGGGACTATACCCTG
TACTCACCACCGCCGCCTGCAGGGGGTGCCATTCTCAGCTTTATCCTCAACGTGCTAAGA
GGGTTCAACTTCTCAACAGAGTCTATGGCCAGGCCTGAAGGGAGGGTGAACGTGTACCAC
CACCTTGTAGAGACGCTCAAGTTTGCCAAGGGGCAGAGGTGGAGGCTGGGGGACCCTCGA
AGCCACCCGAAGCTCCAGAATGCCTCCCGGGACCTGCTGGGGGAGACCCTGGCCCAGCTC
ATCCGCCAACAGATCGATGGCCGGGGGGACCACCAGCTCAGCCACTACAGCTTGGCCGAG
GCCTGGGGCCACGGGACAGGCACGTCCCATGTGTCTGTGCTGGGGGAGGATGGCAGCGCC
GTGGCTGCCACCAGCACCATCAACACACCCTTTGGAGCGATGGTGTATTCACCACGGACA
GGCATCATCCTCAACAACGAGCTCCTGGACTTATGCGAGCGATGCCCCCGGGGTTCCGGC
ACCACCCCCTCACCTGCAGTGAGTGGAGACAGGGTGGGTGGAGCTCCCGGAAGGTGCTGG
CCCCCAGTTCCAGGCGAGCGTTCCCCATCCTCCATGGTGCCCTCCATCTTGATCAACAAA
GCCCAGGGGTCGAAGCTAGTGATTGGCGGGGCTGGCGGGGAGCTCATCATCTCTGCTGTG
GCCCAGGCCATCATGAGCAAGCTGTGGCTTGGCTTTGACCTGAGAGCGGCCATTGCAGCC
CCCATCCTGCATGTCAACAGCAAGGGCTGTGTGGAGTACGAGCCCAACTTCAGCCAGGAG
GTGCAGAGGGGACTCCAAGACCGTGGCCAGAACCAGACCCAGAGGCCCTTCTTCCTGAAC
GTGGTCCAGGCTGTGTCCCAGGAGGGGGCCTGTGTGTACGCCGTCTCGGACCTGAGGAAG
AGTGGGGAGGCCGCAGGCTACTAA
Enzyme 39 GenBank Gene ID BC073999 Link Image
Enzyme 39 GeneCard ID Q6GMP0 Link Image
Enzyme 39 GenAtlas ID GGT5 Link Image
Enzyme 39 HGNC ID HGNC:4260 Link Image
Enzyme 39 Chromosome Location 22
Enzyme 39 Locus 22q11.23
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 15211
Enzyme 40 Name Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
Enzyme 40 Synonyms Not Available
Enzyme 40 Gene Name GSTA3
Enzyme 40 Protein Sequence >Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
Enzyme 40 Number of Residues 222
Enzyme 40 Molecular Weight 25302
Enzyme 40 Theoretical pI 9.69
Enzyme 40 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Not Available
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 114731581 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q068V6 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name Q068V6_HUMAN Link Image
Enzyme 40 PDB ID 1TDI Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >669 bp
ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA
Enzyme 40 GenBank Gene ID DQ993361 Link Image
Enzyme 40 GeneCard ID Q068V6 Link Image
Enzyme 40 GenAtlas ID GSTA3 Link Image
Enzyme 40 HGNC ID HGNC:4628 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References Not Available
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 15212
Enzyme 41 Name cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
Enzyme 41 Synonyms Not Available
Enzyme 41 Gene Name GSTM4
Enzyme 41 Protein Sequence >cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDF
EKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
Enzyme 41 Number of Residues 218
Enzyme 41 Molecular Weight 25562
Enzyme 41 Theoretical pI 5.69
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Not Available
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function Not Available
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 158257192 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID A8K765 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name A8K765_HUMAN Link Image
Enzyme 41 PDB ID 4GTU Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
Enzyme 41 GenBank Gene ID AK291880 Link Image
Enzyme 41 GeneCard ID A8K765 Link Image
Enzyme 41 GenAtlas ID Not Available
Enzyme 41 HGNC ID Not Available
Enzyme 41 Chromosome Location Not Available
Enzyme 41 Locus Not Available
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References Not Available
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 15213
Enzyme 42 Name LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
Enzyme 42 Synonyms Not Available
Enzyme 42 Gene Name LOC51064
Enzyme 42 Protein Sequence >LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
Enzyme 42 Number of Residues 226
Enzyme 42 Molecular Weight 25497
Enzyme 42 Theoretical pI 8.69
Enzyme 42 GO Classification
Function
  • catalytic activity
  • disulfide oxidoreductase activity
  • oxidoreductase activity
  • protein disulfide oxidoreductase activity
Process
Component
  • cell
  • periplasmic space
  • periplasmic space (sensu Gram-negative Bacteria)
Enzyme 42 General Function Not Available
Enzyme 42 Specific Function Not Available
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 158260183 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q6FII1 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name Q6FII1_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
Enzyme 42 GenBank Gene ID AK289580 Link Image
Enzyme 42 GeneCard ID Q6FII1 Link Image
Enzyme 42 GenAtlas ID LOC51064 Link Image
Enzyme 42 HGNC ID HGNC:16906 Link Image
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 15214
Enzyme 43 Name cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
Enzyme 43 Synonyms Not Available
Enzyme 43 Gene Name MGST1
Enzyme 43 Protein Sequence >cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAK
KYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIA
YLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL
Enzyme 43 Number of Residues 155
Enzyme 43 Molecular Weight 17599
Enzyme 43 Theoretical pI 9.71
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Not Available
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function Not Available
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 158255732 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID A8K533 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name A8K533_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >468 bp
ATGGTTGACCTCACCCAGGTAATGGATGATGAAGTATTCATGGCTTTTGCATCCTATGCA
ACAATTATTCTTTCAAAAATGATGCTTATGAGTACTGCAACTGCATTCTATAGATTGACA
AGAAAGGTTTTTGCCAATCCAGAAGACTGTGTAGCATTTGGCAAAGGTGAAAATGCCAAG
AAGTATCTTCGAACAGATGACAGAGTAGAACGTGTACGCAGAGCCCACCTGAATGACCTT
GAAAATATTATTCCATTTCTTGGAATTGGCCTCCTGTATTCCTTGAGTGGTCCCGACCCC
TCTACAGCCATCCTGCACTTCAGACTATTTGTCGGAGCACGGATCTACCACACCATTGCA
TATTTGACACCCCTTCCCCAGCCAAATAGAGCTTTGAGTTTTTTTGTTGGATATGGAGTT
ACTCTTTCCATGGCTTACAGGTTGCTGAAAAGTAAATTGTACCTGTAA
Enzyme 43 GenBank Gene ID AK291148 Link Image
Enzyme 43 GeneCard ID A8K533 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location 12
Enzyme 43 Locus 12p12.3-p12.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References Not Available
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 16491
Enzyme 44 Name cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum)
Enzyme 44 Synonyms Not Available
Enzyme 44 Gene Name TXNDC12
Enzyme 44 Protein Sequence >cDNA PSEC0100 fis, clone NT2RP2002927, highly similar to Thioredoxin domain-containing protein 12 (Thioredoxin domain containing 12) (Endoplasmic reticulum)
METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVI
IHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDP
SGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL
Enzyme 44 Number of Residues 172
Enzyme 44 Molecular Weight 19206
Enzyme 44 Theoretical pI 5.10
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Not Available
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function Not Available
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein Not Available
Enzyme 44 UniProtKB/Swiss-Prot ID B3KQS0 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name B3KQS0_HUMAN Link Image
Enzyme 44 PDB ID 1SEN Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence Not Available
Enzyme 44 GenBank Gene ID AK075409 Link Image
Enzyme 44 GeneCard ID B3KQS0 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location Not Available
Enzyme 44 Locus Not Available
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References Not Available
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 16492
Enzyme 45 Name cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name GSTA4
Enzyme 45 Protein Sequence >cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
Enzyme 45 Number of Residues 222
Enzyme 45 Molecular Weight 25705
Enzyme 45 Theoretical pI 8.72
Enzyme 45 GO Classification
Function
  • catalytic activity
  • glutathione transferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • metabolism
  • physiological process
Component
Enzyme 45 General Function Not Available
Enzyme 45 Specific Function Not Available
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein Not Available
Enzyme 45 UniProtKB/Swiss-Prot ID B2RD15 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name B2RD15_HUMAN Link Image
Enzyme 45 PDB ID 1GUM Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence Not Available
Enzyme 45 GenBank Gene ID AK315369 Link Image
Enzyme 45 GeneCard ID B2RD15 Link Image
Enzyme 45 GenAtlas ID Not Available
Enzyme 45 HGNC ID Not Available
Enzyme 45 Chromosome Location Not Available
Enzyme 45 Locus Not Available
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References Not Available
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 16493
Enzyme 46 Name cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name MGST3
Enzyme 46 Protein Sequence >cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRA
HQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSI
ALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH
Enzyme 46 Number of Residues 152
Enzyme 46 Molecular Weight 16516
Enzyme 46 Theoretical pI 9.68
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Not Available
Enzyme 46 Specific Function Not Available
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID B2R592 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name B2R592_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence Not Available
Enzyme 46 GenBank Gene ID AK312103 Link Image
Enzyme 46 GeneCard ID B2R592 Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location Not Available
Enzyme 46 Locus Not Available
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References Not Available
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 16494
Enzyme 47 Name cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name Not Available
Enzyme 47 Protein Sequence >cDNA FLJ32487 fis, clone SKNSH1000002, highly similar to Prostaglandin E synthase 2 (EC 5.3.99.3)
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLG
AAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRALL
DFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQ
PLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADD
WLVHLIFPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQ
DNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQ
PWYLRVERAITEASPAH
Enzyme 47 Number of Residues 377
Enzyme 47 Molecular Weight 41970
Enzyme 47 Theoretical pI 9.50
Enzyme 47 GO Classification
Function
  • electron transporter activity
  • transporter activity
Process
  • cell homeostasis
  • cell redox homeostasis
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • homeostasis
  • metabolism
  • physiological process
Component
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Not Available
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions
  • (5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13- dienoate = (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate [RN:R02265] ALL_REAC R02265
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein Not Available
Enzyme 47 UniProtKB/Swiss-Prot ID B3KPZ2 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name B3KPZ2_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence Not Available
Enzyme 47 GenBank Gene ID AK057049 Link Image
Enzyme 47 GeneCard ID B3KPZ2 Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location Not Available
Enzyme 47 Locus Not Available
Enzyme 47 SNPs Not Available
Enzyme 47 General References Not Available
Enzyme 47 Metabolite References Not Available