We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for Hydrochloric acid (HMDB02306)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:47
Update Date 2008-12-08 00:21:06
Accession Number HMDB02306
Secondary Accession Numbers HMDB02162
Common Name Hydrochloric acid
Description Hydrochloric acid constitutes the majority of gastric acid, the human digestive fluid. In a complex process and at a large energetic burden, it is secreted by parietal cells (also known as oxyntic cells). These cells contain an extensive secretory network (called canaliculi) from which the HCl is secreted into the lumen of the stomach. They are part of the epithelial fundic glands (also known as oxyntic glands) in the stomach. The chemical compound hydrochloric acid is the aqueous (water-based) solution of hydrogen chloride gas (HCl). It is a strong acid, the major component of gastric acid and of wide industrial use. Hydrochloric acid must be handled with appropriate safety precautions because it is a highly corrosive liquid. Hydrochloric acid, or muriatic acid by its historical but still occasionally used name, has been an important and frequently used chemical from early history and was discovered by the alchemist Jabir ibn Hayyan around the year 800. Hydrogen chloride, also known under the name HCl, is a highly corrosive and toxic colorless gas that forms white fumes on contact with humidity. These fumes consist of hydrochloric acid which forms when hydrogen chloride dissolves in water. The hydrogen chloride molecule HCl is a simple diatomic molecule consisting of a hydrogen atom H and a chlorine atom Cl connected with a covalent single bond. Since the chlorine atom is much more electronegative than the hydrogen atom, the covalent bond between the atoms is quite polar. Hydrogen chloride forms corrosive hydrochloric acid on contact with body tissue. Inhalation of the fumes can cause coughing, choking, inflammation of the nose, throat, and upper respiratory tract, and in severe cases, pulmonary edema, circulatory system failure, and death. Skin contact can cause redness, pain, and severe skin burns. Hydrogen chloride may cause severe burns to the eye and permanent eye damage.
Synonyms
  1. Hydrogen chloride anhydrous [UN1050] [Poison gas]
  2. Hydrogen chloric anhydrous
  3. Marine acid
  4. [HCL]
  5. Hydrochloric acid (JP15/NF)
  6. Hydrogen chloride (acid)
  7. Chlorane
  8. Hydrochloric acid [jan]
  9. Aqueous hydrogen chloride
  10. Hydrochloric acid gas
  11. Chlorohydric acid
  12. Spirit of salt
  13. Muriatic acid
  14. HCL]
  15. Hydrogen chloride (HCL)
  16. anhydrous Hydrochloric acid
Chemical IUPAC Name hydrogen chloride
Chemical Formula ClH
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Inorganic compounds
Class
  • Inorganic Ions and Gases
Sub Class
  • Anions
Family
  • Mammalian Metabolite
Species
Biofunction
  • Osmolyte, enzyme cofactor, signalling
Application
Source
  • Endogenous
Average Molecular Weight 36.461
Monoisotopic Molecular Weight 35.976681
Isomeric SMILES Cl
Canonical SMILES Cl
KEGG Compound ID C01327 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Hydrochloric acid Link Image
NuGOwiki Link HMDB02306 Link Image
Metagene Link HMDB02306 Link Image
METLIN ID Not Available
PubChem Compound 313 Link Image
PubChem Substance 2784 Link Image
ChEBI ID 17883 Link Image
CAS Registry Number 7647-01-0
InChI Identifier InChI=1/ClH/h1H
Synthesis Reference Suzuta, Tetsuya; Mori, Yasuhiko; Abe, Tadashi. method to produce chlorine and hydrochloric acid. Jpn. Kokai Tokkyo Koho (2005), 13 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways Not Available
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Glutathione S-transferase Mu 2
  2. Glutathione S-transferase Mu 1
  3. Glutathione S-transferase Mu 3
  4. Glutathione S-transferase A1
  5. Glutathione S-transferase theta-2
  6. Glutathione S-transferase Mu 5
  7. Microsomal glutathione S-transferase 2
  8. Glutathione transferase omega-1
  9. Glutathione S-transferase A5
  10. Glutathione S-transferase A2
  11. Glutathione transferase omega-2
  12. Glutathione S-transferase theta-1
  13. Glutathione S-transferase P
  14. Uncharacterized protein GSTZ1
  15. Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
  16. cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
  17. LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
  18. 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)
  19. cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
  20. cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 6088
Enzyme 1 Name Glutathione S-transferase Mu 2
Enzyme 1 Synonyms
  1. GSTM2-2
  2. GST class-mu 2
Enzyme 1 Gene Name GSTM2
Enzyme 1 Protein Sequence >Glutathione S-transferase Mu 2
MPMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILENQFMDSRMQLAKLCYDPDF
EKLKPEYLQALPEMLKLYSQFLGKQPWFLGDKITFVDFIAYDVLERNQVFEPSCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFTKMAVWGNK
Enzyme 1 Number of Residues 218
Enzyme 1 Molecular Weight 25745
Enzyme 1 Theoretical pI 6.29
Enzyme 1 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 1 General Function Not Available
Enzyme 1 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 1 Pathways
Enzyme 1 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-16
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 183301 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P28161 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GSTM2_HUMAN Link Image
Enzyme 1 PDB ID 1XW5 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >657 bp
ATGCCCATGACACTGGGGTACTGGAACATCCGCGGGCTGGCCCATTCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGACTCACAAGATCACCCAGAGCAATGCCATCCTGCGGTACATT
GCCCGCAAGCACAACCTGTGCGGGGAATCAGAAAAGGAGCAGATTCGCGAAGACATTTTG
GAGAACCAGTTTATGGACAGCCGTATGCAGCTGGCCAAACTCTGCTATGACCCAGATTTT
GAGAAACTGAAACCAGAATACCTGCAGGCACTCCCTGAAATGCTGAAGCTCTACTCACAG
TTTCTGGGGAAGCAGCCATGGTTTCTTGGGGACAAGATCACCTTTGTGGATTTCATCGCT
TATGATGTCCTTGAGAGAAACCAAGTATTTGAGCCCAGCTGCCTGGATGCCTTCCCAAAC
CTGAAGGACTTCATCTCCCGATTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCACAAAGATGGCTGTCTGGGGCAACAAGTAG
Enzyme 1 GenBank Gene ID M63509 Link Image
Enzyme 1 GeneCard ID GSTM2 Link Image
Enzyme 1 GenAtlas ID GSTM2 Link Image
Enzyme 1 HGNC ID HGNC:4634 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6091
Enzyme 2 Name Glutathione S-transferase Mu 1
Enzyme 2 Synonyms
  1. GSTM1-1
  2. GST class-mu 1
  3. GSTM1a-1a
  4. GSTM1b-1b
  5. HB subunit 4
  6. GTH4
Enzyme 2 Gene Name GSTM1
Enzyme 2 Protein Sequence >Glutathione S-transferase Mu 1
MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPN
LKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK
Enzyme 2 Number of Residues 218
Enzyme 2 Molecular Weight 25712
Enzyme 2 Theoretical pI 6.67
Enzyme 2 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 2 General Function Not Available
Enzyme 2 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 2 Pathways
Enzyme 2 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-16
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 31924 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P09488 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GSTM1_HUMAN Link Image
Enzyme 2 PDB ID 1XWK Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >657 bp
ATGCCCATGATACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTATGAGGAAAAGAAGTACACGATGGGGGACGCTCCTGAT
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCTTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGACCATGGACAACCATATGCAGCTGGGCATGATCTGCTACAATCCAGAATTT
GAGAAACTGAAGCCAAAGTACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAAACAAGATCACTTTTGTAGATTTTCTCGTC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAGACCTGTGTTCTCAAAGATGGCTGTCTGGGGCAACAAGTAG
Enzyme 2 GenBank Gene ID X08020 Link Image
Enzyme 2 GeneCard ID GSTM1 Link Image
Enzyme 2 GenAtlas ID GSTM1 Link Image
Enzyme 2 HGNC ID HGNC:4632 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6095
Enzyme 3 Name Glutathione S-transferase Mu 3
Enzyme 3 Synonyms
  1. GSTM3-3
  2. GST class-mu 3
  3. hGSTM3-3
Enzyme 3 Gene Name GSTM3
Enzyme 3 Protein Sequence >Glutathione S-transferase Mu 3
MSCESSMVLGYWDIRGLAHAIRLLLEFTDTSYEEKRYTCGEAPDYDRSQWLDVKFKLDLD
FPNLPYLLDGKNKITQSNAILRYIARKHNMCGETEEEKIRVDIIENQVMDFRTQLIRLCY
SSDHEKLKPQYLEELPGQLKQFSMFLGKFSWFAGEKLTFVDFLTYDILDQNRIFDPKCLD
EFPNLKAFMCRFEALEKIAAYLQSDQFCKMPINNKMAQWGNKPVC
Enzyme 3 Number of Residues 225
Enzyme 3 Molecular Weight 26560
Enzyme 3 Theoretical pI 5.19
Enzyme 3 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 3 General Function Not Available
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 306820 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P21266 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GSTM3_HUMAN Link Image
Enzyme 3 PDB ID 3GTU Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >678 bp
ATGTCGTGCGAGTCGTCTATGGTTCTCGGGTACTGGGATATTCGTGGGCTGGCGCACGCC
ATCCGCCTGCTCCTGGAGTTCACGGATACCTCTTATGAGGAGAAACGGTACACGTGCGGG
GAAGCTCCTGACTATGATCGAAGCCAATGGCTGGATGTGAAATTCAAGCTAGACCTGGAC
TTTCCTAATCTGCCCTACCTCCTGGATGGGAAGAACAAGATCACCCAGAGCAATGCCATC
TTGCGCTACATCGCTCGCAAGCACAACATGTGTGGTGAGACTGAAGAAGAAAAGATTCGA
GTGGACATCATAGAGAACCAAGTAATGGATTTCCGCACACAACTGATAAGGCTCTGTTAC
AGCTCTGACCACGAAAAACTGAAGCCTCAGTACTTGGAAGAGCTACCTGGACAACTGAAA
CAATTCTCCATGTTTCTGTGGAAATTCTCATGGTTTGCCGGGGAAAAGCTCACCTTTGTG
GATTTTCTCACCTATGATATCTTGGATCAGAACCGTATATTTGACCCCAAGTGCCTGGAT
GAGTTCCCAAACCTGAAGGCTTTCATGTGCCGTTTTGAGGCTTTGGAGAAAATCGCTGCC
TACTTACAGTCTGATCAGTTCTGCAAGATGCCCATCAACAACAAGATGGCCCAGTGGGGC
AACAAGCCTGTATGCTGA
Enzyme 3 GenBank Gene ID J05459 Link Image
Enzyme 3 GeneCard ID GSTM3 Link Image
Enzyme 3 GenAtlas ID GSTM3 Link Image
Enzyme 3 HGNC ID HGNC:4635 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6096
Enzyme 4 Name Glutathione S-transferase A1
Enzyme 4 Synonyms
  1. GTH1
  2. HA subunit 1
  3. GST- epsilon
  4. GSTA1-1
  5. GST class-alpha member 1
Enzyme 4 Gene Name GSTA1
Enzyme 4 Protein Sequence >Glutathione S-transferase A1
MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAK
LALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF
Enzyme 4 Number of Residues 222
Enzyme 4 Molecular Weight 25631
Enzyme 4 Theoretical pI 9.34
Enzyme 4 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 4 General Function Not Available
Enzyme 4 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 4 Pathways
Enzyme 4 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 306809 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P08263 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GSTA1_HUMAN Link Image
Enzyme 4 PDB ID 1K3Y Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTTCAATGCACGGGGCAGAATGGAGTCCACCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAGAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTCCTTCTGCCCGTATGTCCACCTGAGGAAAAAGATGCCAAG
CTTGCCTTGATCAAGGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCATCTG
GTGGAACTTCTCTACTACGTCGAGGAGCTTGACTCCAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 4 GenBank Gene ID M15872 Link Image
Enzyme 4 GeneCard ID GSTA1 Link Image
Enzyme 4 GenAtlas ID GSTA1 Link Image
Enzyme 4 HGNC ID HGNC:4626 Link Image
Enzyme 4 Chromosome Location 6
Enzyme 4 Locus 6p12.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6098
Enzyme 5 Name Glutathione S-transferase theta-2
Enzyme 5 Synonyms
  1. GST class-theta-2
Enzyme 5 Gene Name GSTT2
Enzyme 5 Protein Sequence >Glutathione S-transferase theta-2
MGLELFLDLVSQPSRAVYIFAKKNGIPLELRTVDLVKGQHKSKEFLQINSLGKLPTLKDG
DFILTESSAILIYLSCKYQTPDHWYPSDLQARARVHEYLGWHADCIRGTFGIPLWVQVLG
PLIGVQVPEEKVERNRTAMDQALQWLEDKFLGDRPFLAGQQVTLADLMALEELMQPVALG
YELFEGRPRLAAWRGRVEAFLGAELCQEAHSIILSILEQAAKKTLPTPSPEAYQAMLLRI
ARIP
Enzyme 5 Number of Residues 244
Enzyme 5 Molecular Weight 27507
Enzyme 5 Theoretical pI 6.36
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 5 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity
Enzyme 5 Pathways
Enzyme 5 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-16
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 601918 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P30712 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GSTT2_HUMAN Link Image
Enzyme 5 PDB ID 3LJR Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >735 bp
ATGGGCCTAGAGCTGTTTCTTGACCTGGTGTCCCAGCCCAGCCGCGCCGTCTACATCTTC
GCCAAGAAGAATGGCATCCCCTTAGAGCTGCGCACCGTGGATTTGGTCAAAGGGCAGCAC
AAGAGCAAGGAGTTCTTGCAGATCAACAGCCTGGGGAAACTGCCGACGCTCAAGGATGGT
GATTTCATCTTGACCGAAAGCTCGGCCATCCTGATTTACCTGAGCTGTAAGTACCAGACG
CCGGACCACTGGTATCCATCTGACCTGCAGGCTCGTGCCCGTGTTCATGAGTACCTGGGC
TGGCATGCCGACTGCATCCGTGGCACCTTTGGTATACCCCTGTGGGTCCAGGTGTTGGGG
CCACTCATTGGGGTCCAGGTGCCCGAGGAGAAGGTGGAACGCAACAGGACTGCCATGGAC
CAGGCCCTGCAATGGCTGGAGGACAAGTTCCTGGGGGACAGGCCCTTCCTCGCTGGCCAG
CAGGTGACACTGGCTGATCTCATGGCCCTGGAGGAGCTGATGCAGCCGGTGGCTCTCGGC
TACGAACTGTTTGAGGGACGGCCACGACTGGCAGCATGGCGTGGACGAGTGGAGGCTTTC
CTGGGTGCTGAGCTATGCCAGGAGGCCCACAGCATCATCTTGAGCATCCTGGAACAGGCG
GCCAAGAAAACCCTCCCAACACCCTCACCAGAGGCCTATCAGGCTATGCTGCTTCGAATC
GCCAGGATCCCCTGA
Enzyme 5 GenBank Gene ID L38503 Link Image
Enzyme 5 GeneCard ID GSTT2 Link Image
Enzyme 5 GenAtlas ID GSTT2 Link Image
Enzyme 5 HGNC ID HGNC:4642 Link Image
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q11.2|22q11.23
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6101
Enzyme 6 Name Glutathione S-transferase Mu 5
Enzyme 6 Synonyms
  1. GSTM5-5
  2. GST class-mu 5
Enzyme 6 Gene Name GSTM5
Enzyme 6 Protein Sequence >Glutathione S-transferase Mu 5
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNL
PYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDF
EKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLN
LKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
Enzyme 6 Number of Residues 218
Enzyme 6 Molecular Weight 25675
Enzyme 6 Theoretical pI 7.49
Enzyme 6 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 6 General Function Not Available
Enzyme 6 Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles
Enzyme 6 Pathways
Enzyme 6 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-16
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 468260 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P46439 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name GSTM5_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >657 bp
ATGCCCATGACTCTGGGGTACTGGGACATCCGTGGGCTGGCCCACGCCATCCGCTTGCTC
CTGGAATACACAGACTCAAGCTATGTGGAAAAGAAGTACACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAATGCCATCCTGCGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGTTATGGATAACCACATGGAGCTGGTCAGACTGTGCTATGACCCAGATTTT
GAGAAACTGAAGCCAAAATACTTGGAGGAACTCCCTGAAAAGCTAAAGCTCTACTCAGAG
TTTCTGGGGAAGCGGCCATGGTTTGCAGGAGACAAGATCACCTTTGTGGATTTCCTTGCC
TATGATGTCCTTGACATGAAGCGTATATTTGAGCCCAAGTGCTTGGACGCCTTCCTAAAC
TTGAAGGACTTCATCTCCCGCTTTGAGGGTTTGAAGAAGATCTCTGCCTACATGAAGTCC
AGCCAATTCCTCCGAGGTCTTTTGTTTGGAAAGTCAGCTACATGGAACAGCAAATAG
Enzyme 6 GenBank Gene ID L02321 Link Image
Enzyme 6 GeneCard ID GSTM5 Link Image
Enzyme 6 GenAtlas ID GSTM5 Link Image
Enzyme 6 HGNC ID HGNC:4637 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6102
Enzyme 7 Name Microsomal glutathione S-transferase 2
Enzyme 7 Synonyms
  1. Microsomal GST- 2
  2. Microsomal GST-II
Enzyme 7 Gene Name MGST2
Enzyme 7 Protein Sequence >Microsomal glutathione S-transferase 2
MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFY
PIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTL
LGALGIANSFLDEYLDLNIAKKLRRQF
Enzyme 7 Number of Residues 147
Enzyme 7 Molecular Weight 16621
Enzyme 7 Theoretical pI 9.88
Enzyme 7 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 7 General Function Not Available
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-23
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1747521 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q99735 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name MGST2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >444 bp
ATGGCCGGGAACTCGATCCTGCTGGCTGCTGTCTCTATTCTCTCGGCCTGTCAGCAAAGT
TATTTTGCTTTGCAAGTTGGAAAGGCAAGATTAAAATACAAAGTTACGCCCCCAGCAGTC
ACTGGGTCACCAGAGTTTGAGAGAGTATTTCGGGCACAACAAAACTGTGTGGAGTTTTAT
CCTATATTCATAATTACATTGTGGATGGCTGGGTGGTATTTCAACCAAGTTTTTGCTACT
TGTCTGGGTCTGGTGTACATATATGGCCGTCACCTATACTTCTGGGGATATTCAGAAGCT
GCTAAAAAACGGATCACCGGTTTCCGACTGAGTCTGGGGATTTTGGCCTTGTTGACCCTC
CTAGGTGCCCTGGGAATTGCAAACAGCTTTCTGGATGAATATCTGGACCTCAATATTGCC
AAGAAACTGAGGCGGCAATTCTAA
Enzyme 7 GenBank Gene ID U77604 Link Image
Enzyme 7 GeneCard ID MGST2 Link Image
Enzyme 7 GenAtlas ID MGST2 Link Image
Enzyme 7 HGNC ID HGNC:7063 Link Image
Enzyme 7 Chromosome Location 4
Enzyme 7 Locus 4q28.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6103
Enzyme 8 Name Glutathione transferase omega-1
Enzyme 8 Synonyms
  1. GSTO 1-1
Enzyme 8 Gene Name GSTO1
Enzyme 8 Protein Sequence >Glutathione transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
Enzyme 8 Number of Residues 241
Enzyme 8 Molecular Weight 27566
Enzyme 8 Theoretical pI 6.54
Enzyme 8 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 8 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 8 Specific Function Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities
Enzyme 8 Pathways
Enzyme 8 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 2393722 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P78417 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GSTO1_HUMAN Link Image
Enzyme 8 PDB ID 1EEM Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >726 bp
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA
Enzyme 8 GenBank Gene ID U90313 Link Image
Enzyme 8 GeneCard ID GSTO1 Link Image
Enzyme 8 GenAtlas ID GSTO1 Link Image
Enzyme 8 HGNC ID HGNC:13312 Link Image
Enzyme 8 Chromosome Location 10
Enzyme 8 Locus 10q25.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6104
Enzyme 9 Name Glutathione S-transferase A5
Enzyme 9 Synonyms
  1. Glutathione S-transferase A5-5
  2. GST class-alpha member 5
Enzyme 9 Gene Name GSTA5
Enzyme 9 Protein Sequence >Glutathione S-transferase A5
MAEKPKLHYSNARGSMESIRWLLAAAGVELEEKFLESAEDLDKLRNDGSLLFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDMKERALIDMYTEGIVDLTEMILLLLICQPEERDAK
TALVKEKIKNRYFPAFEKVLKSHRQDYLVGNKLSWADIHLVELFYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSQRKPPMDEKSLEEARKIFRF
Enzyme 9 Number of Residues 222
Enzyme 9 Molecular Weight 25722
Enzyme 9 Theoretical pI 8.37
Enzyme 9 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 9 General Function Not Available
Enzyme 9 Specific Function RX + glutathione = HX + R-S-glutathione
Enzyme 9 Pathways
Enzyme 9 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 23197582 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q7RTV2 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name GSTA5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATGCACGGGGCAGTATGGAGTCCATTCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTGGAAGAGAAATTTCTAGAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGGAGTTTGCTGTTCCAGCAAGTACCAATGGTTGAGATT
GACGGGATGAAGCTGGTGCAGACCAGAGCCATTCTTAACTACATTGCCAGCAAATACAAC
CTTTATGGGAAAGACATGAAGGAGAGAGCCCTGATTGATATGTACACAGAAGGTATAGTA
GATTTGACTGAAATGATCCTTCTTCTGCTCATATGTCAACCAGAGGAAAGAGATGCCAAG
ACTGCCTTGGTCAAAGAGAAAATAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACAGACAAGACTACCTTGTTGGCAACAAGCTGAGCTGGGCTGACATTCACCTG
GTGGAACTTTTCTACTACGTGGAAGAGCTTGACTCGAGTCTTATCTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTGCAGCCT
GGCAGCCAGAGAAAGCCTCCCATGGATGAGAAATCTTTAGAAGAAGCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 9 GenBank Gene ID BK000212 Link Image
Enzyme 9 GeneCard ID GSTA5 Link Image
Enzyme 9 GenAtlas ID GSTA5 Link Image
Enzyme 9 HGNC ID HGNC:19662 Link Image
Enzyme 9 Chromosome Location 6
Enzyme 9 Locus 6p12.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 6105
Enzyme 10 Name Glutathione S-transferase A2
Enzyme 10 Synonyms
  1. GTH2
  2. HA subunit 2
  3. GST- gamma
  4. GSTA2-2
  5. GST class-alpha member 2
Enzyme 10 Gene Name GSTA2
Enzyme 10 Protein Sequence >Glutathione S-transferase A2
MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAK
LALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPL
LKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF
Enzyme 10 Number of Residues 222
Enzyme 10 Molecular Weight 25664
Enzyme 10 Theoretical pI 9.07
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
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 306811 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P09210 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name GSTA2_HUMAN Link Image
Enzyme 10 PDB ID 1AGS Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >669 bp
ATGGCAGAGAAGCCCAAGCTCCACTACTCCAATATACGGGGCAGAATGGAGTCCATCCGG
TGGCTCCTGGCTGCAGCTGGAGTAGAGTTTGAAGAGAAATTTATAAAATCTGCAGAAGAT
TTGGACAAGTTAAGAAATGATGGATATTTGATGTTCCAGCAAGTGCCAATGGTTGAGATT
GATGGGATGAAGCTGGTGCAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTATGGGAAAGACATAAAGGAGAAAGCCCTGATTGATATGTATATAGAAGGTATAGCA
GATTTGGGTGAAATGATCCTTCTTCTGCCCTTTACTCAACCTGAGGAACAAGATGCCAAG
CTTGCCTTGATCCAAGAGAAAACAAAAAATCGCTACTTCCCTGCCTTTGAAAAAGTCTTA
AAGAGCCACGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTCACCTG
GTGGAACTTCTCTACTACGTGGAAGAGCTTGACTCTAGCCTTATTTCCAGCTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGTAACCTGCCCACAGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCATGGATGAGAAATCTTTAGAAGAATCAAGGAAGATTTTC
AGGTTTTAA
Enzyme 10 GenBank Gene ID M16594 Link Image
Enzyme 10 GeneCard ID GSTA2 Link Image
Enzyme 10 GenAtlas ID GSTA2 Link Image
Enzyme 10 HGNC ID HGNC:4627 Link Image
Enzyme 10 Chromosome Location 6
Enzyme 10 Locus 6p12.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 6112
Enzyme 11 Name Glutathione transferase omega-2
Enzyme 11 Synonyms
  1. GSTO-2
Enzyme 11 Gene Name GSTO2
Enzyme 11 Protein Sequence >Glutathione transferase omega-2
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKP
EWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELF
CKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWP
WFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDF
GLC
Enzyme 11 Number of Residues 243
Enzyme 11 Molecular Weight 28254
Enzyme 11 Theoretical pI 7.62
Enzyme 11 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 11 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 11 Specific Function RX + glutathione = HX + R-S-glutathione
Enzyme 11 Pathways
Enzyme 11 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 37777744 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9H4Y5 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name GSTO2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >732 bp
ATGTCTGGGGATGCGACCAGGACCCTGGGGAAAGGAAGCCAGCCCCCAGGGCCAGTCCCG
GAGGGGCTGATCCGCATCTACAGCATGAGGTTCTGCCCCTATTCTCACAGGACCCGCCTC
GTCCTCAAGGCCAAAGACATCAGACATGAAGTGGTCAACATTAACCTGAGAAACAAGCCT
GAATGGTACTATACAAAGCACCCTTTTGGCCACATTCCTGTCCTGGAGACCAGCCAATGT
CAACTGATCTATGAATCTGTTATTGCTTGTGAGTACCTGGATGATGCTTATCCAGGAAGG
AAGCTGTTTCCATATGACCCTTATGAACGAGCTCGCCAAAAGATGTTATTGGAGCTATTT
TGTAAGGTCCCACATTTGACCAAGGAGTGCCTGGTAGCGTTGAGATGTGGGAGAGAATGC
ACTAATCTGAAGGCAGCCCTGCGTCAGGAATTCAGCAACCTGGAAGAGATTCTTGAGTAT
CAGAACACCACCTTCTTTGGTGGAACCTGTATATCCATGATTGATTACCTCCTCTGGCCC
TGGTTTGAGCGGCTGGATGTGTATGGGATACTGGACTGTGTGAGCCACACGCCAGCCCTG
CGGCTCTGGATATCAGCCATGAAGTGGGACCCCACAGTCTGTGCTCTTCTCATGGATAAG
AGCATTTTCCAGGGCTTCTTGAATCTCTATTTTCAGAACAACCCTAATGCCTTTGACTTT
GGGCTGTGCTGA
Enzyme 11 GenBank Gene ID AY350731 Link Image
Enzyme 11 GeneCard ID GSTO2 Link Image
Enzyme 11 GenAtlas ID GSTO2 Link Image
Enzyme 11 HGNC ID HGNC:23064 Link Image
Enzyme 11 Chromosome Location 10
Enzyme 11 Locus 10q25.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6113
Enzyme 12 Name Glutathione S-transferase theta-1
Enzyme 12 Synonyms
  1. GST class-theta-1
  2. Glutathione transferase T1-1
Enzyme 12 Gene Name GSTT1
Enzyme 12 Protein Sequence >Glutathione S-transferase theta-1
MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDG
DFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMF
PVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGA
GCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR
Enzyme 12 Number of Residues 240
Enzyme 12 Molecular Weight 27335
Enzyme 12 Theoretical pI 7.60
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 12 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 12 Pathways
Enzyme 12 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-16
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 510905 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P30711 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name GSTT1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >723 bp
ATGGGTCTGGAGCTCTACCTGGACCTGCTGTCCCAGCCCTGCCGCGCTGTTTACATCTTT
GCCAAGAAGAACGACATTCCCTTCGAGCTGCGCATCGTGGATCTGATTAAAGGTCAGCAC
TTAAGCGATGCCTTTGCCCAGGTGAACCCCCTCAAGAAGGTGCCGGCCTTGAAGGACGGG
GACTTCACCTTGACGGAGAGTGTGGCCATCCTGCTCTACCTGACGCGCAAATATAAGGTC
CCTGACTACTGGTACCCTCAGGACCTGCAGGCCCGTGCCCGTGTGGATGAGTACCTGGCA
TGGCAGCACACGACTCTGCGGAGAAGCTGCCTCCGGGCCTTGTGGCATAAGGTGATGTTC
CCTGTGTTCCTGGGTGGGCCAGTATCTCCCCAGACACTGGCAGCCACCCTGGCAGAGTTG
GATGTGACCCTGCAGTTGCTCGAGGACAAGTTCCTCCAGAACAAGGCCTTCCTTACTGGT
CCTCACATCTCCTTAGCTGACCTCGTAGCCATCACGGAGCTGATGCATCCCGTGGGTGCT
GGCTGCCAAGTCTTCGAAGGCCGACCCAAGCTGGCCACATGGCGGCAGCGCGTGGAGGCA
GCAGTGGGGGAGGACCTCTTCCAGGAGGCCCATGAGGTCATTCTGAAGGCCAAGGACTTC
CCACCTGCAGACCCCACCATAAAGCAGAAGCTGATGCCCTGGGTGCTGGCCATGATCCGG
TGA
Enzyme 12 GenBank Gene ID X79389 Link Image
Enzyme 12 GeneCard ID GSTT1 Link Image
Enzyme 12 GenAtlas ID GSTT1 Link Image
Enzyme 12 HGNC ID HGNC:4641 Link Image
Enzyme 12 Chromosome Location 22
Enzyme 12 Locus 22q11.23
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6115
Enzyme 13 Name Glutathione S-transferase P
Enzyme 13 Synonyms
  1. GST class-pi
  2. GSTP1-1
Enzyme 13 Gene Name GSTP1
Enzyme 13 Protein Sequence >Glutathione S-transferase P
MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGD
LTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYV
KALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAY
VGRLSARPKLKAFLASPEYVNLPINGNGKQ
Enzyme 13 Number of Residues 210
Enzyme 13 Molecular Weight 23356
Enzyme 13 Theoretical pI 5.30
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
Enzyme 13 Pathways
Enzyme 13 Reactions
  • RX + glutathione = HX + R-S-glutathione
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-17
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 31946 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P09211 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name GSTP1_HUMAN Link Image
Enzyme 13 PDB ID 13GS Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >633 bp
ATGCCGCCCTACACCGTGGTCTATTTCCCAGTTCGAGGCCGCTGCGCGGCCCTGCGCATG
CTGCTGGCAGATCAGGGCCAGAGCTGGAAGGAGGAGGTGGTGACCGTGGAGACGTGGCAG
GAGGGCTCACTCAAAGCCTCCTGCCTATACGGGCAGCTCCCCAAGTTCCAGGACGGAGAC
CTCACCCTGTACCAGTCCAATACCATCCTGCGTCACCTGGGCCGCACCCTTGGGCTCTAT
GGGAAGGACCAGCAGGAGGCAGCCCTGGTGGACATGGTGAATGACGGCGTGGAGGACCTC
CGCTGCAAATACATCTCCCTCATCTACACCAACTATGAGGCGGGCAAGGATGACTATGTG
AAGGCACTGCCCGGGCAACTGAAGCCTTTTGAGACCCTGCTGTCCCAGAACCAGGGAGGC
AAGACCTTCATTGTGGGAGACCAGATCTCCTTCGCTGACTACAACCTGCTGGACTTGCTG
CTGATCCATGAGGTCCTAGCCCCTGGCTGCCTGGATGCGTTCCCCCTGCTCTCAGCATAT
GTGGGGCGCCTCAGCGCCCGGCCCAAGCTCAAGGCCTTCCTGGCCTCCCCTGAGTACGTG
AACCTCCCCATCAATGGCAACGGGAAACAGTGA
Enzyme 13 GenBank Gene ID X06547 Link Image
Enzyme 13 GeneCard ID GSTP1 Link Image
Enzyme 13 GenAtlas ID GSTP1 Link Image
Enzyme 13 HGNC ID HGNC:4638 Link Image
Enzyme 13 Chromosome Location 11
Enzyme 13 Locus 11q13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 13120
Enzyme 14 Name Uncharacterized protein GSTZ1
Enzyme 14 Synonyms
  1. Glutathione transferase zeta 1
  2. Maleylacetoacetate isomerase, isoform CRA_a
Enzyme 14 Gene Name GSTZ1
Enzyme 14 Protein Sequence >Uncharacterized protein GSTZ1
MKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQN
LSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAER
FKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
Enzyme 14 Number of Residues 161
Enzyme 14 Molecular Weight 17896
Enzyme 14 Theoretical pI 5.76
Enzyme 14 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 14 General Function Posttranslational modification, protein turnover, chaperones
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID A6NNB8 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name A6NNB8_HUMAN Link Image
Enzyme 14 PDB ID 1FW1 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AC007954 Link Image
Enzyme 14 GeneCard ID A6NNB8 Link Image
Enzyme 14 GenAtlas ID GSTZ1 Link Image
Enzyme 14 HGNC ID HGNC:4643 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 15211
Enzyme 15 Name Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name GSTA3
Enzyme 15 Protein Sequence >Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
Enzyme 15 Number of Residues 222
Enzyme 15 Molecular Weight 25302
Enzyme 15 Theoretical pI 9.69
Enzyme 15 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 15 General Function Not Available
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 114731581 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q068V6 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q068V6_HUMAN Link Image
Enzyme 15 PDB ID 1TDI Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >669 bp
ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA
Enzyme 15 GenBank Gene ID DQ993361 Link Image
Enzyme 15 GeneCard ID Q068V6 Link Image
Enzyme 15 GenAtlas ID GSTA3 Link Image
Enzyme 15 HGNC ID HGNC:4628 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15212
Enzyme 16 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 16 Synonyms Not Available
Enzyme 16 Gene Name GSTM4
Enzyme 16 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 16 Number of Residues 218
Enzyme 16 Molecular Weight 25562
Enzyme 16 Theoretical pI 5.69
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function Not Available
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 158257192 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID A8K765 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name A8K765_HUMAN Link Image
Enzyme 16 PDB ID 4GTU Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >657 bp
ATGTCCATGACACTGGGGTACTGGGACATCCGCGGGCTGGCCCACGCCATCCGCCTGCTC
CTGGAATACACAGACTCAAGCTACGAGGAAAAGAAGTATACGATGGGGGACGCTCCTGAC
TATGACAGAAGCCAGTGGCTGAATGAAAAATTCAAGCTGGGCCTGGACTTTCCCAATCTG
CCCTACTTGATTGATGGGGCTCACAAGATCACCCAGAGCAACGCCATCCTGTGCTACATT
GCCCGCAAGCACAACCTGTGTGGGGAGACAGAAGAGGAGAAGATTCGTGTGGACATTTTG
GAGAACCAGGCTATGGACGTCTCCAATCAGCTGGCCAGAGTCTGCTACAGCCCTGACTTT
GAGAAACTGAAGCCAGAATACTTGGAGGAACTTCCTACAATGATGCAGCACTTCTCACAG
TTCCTGGGGAAGAGGCCATGGTTTGTTGGAGACAAGATCACCTTTGTAGATTTCCTCGCC
TATGATGTCCTTGACCTCCACCGTATATTTGAGCCCAACTGCTTGGACGCCTTTCCAAAT
CTGAAGGACTTCATCTCCCGCTTTGAGGGCTTGGAGAAGATCTCTGCCTACATGAAGTCC
AGCCGCTTCCTCCCAAAACCTCTGTACACAAGGGTGGCTGTCTGGGGCAACAAGTAA
Enzyme 16 GenBank Gene ID AK291880 Link Image
Enzyme 16 GeneCard ID A8K765 Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15213
Enzyme 17 Name LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name LOC51064
Enzyme 17 Protein Sequence >LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLP
RKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRE
LWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGA
FGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL
Enzyme 17 Number of Residues 226
Enzyme 17 Molecular Weight 25497
Enzyme 17 Theoretical pI 8.69
Enzyme 17 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 17 General Function Not Available
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 158260183 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q6FII1 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q6FII1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >681 bp
ATGGGGCCCCTGCCGCGCACCGTGGAGCTCTTCTATGACGTGCTGTCCCCCTACTCCTGG
CTGGGCTTCGAGATCCTGTGCCGGTATCAGAATATCTGGAACATCAACCTGCAGTTGCGG
CCCAGCCTCATAACAGGGATCATGAAAGACAGTGGAAACAAGCCTCCAGGTCTGCTTCCC
CGCAAAGGACTATACATGGCAAATGACTTAAAGCTCCTGAGACACCATCTCCAGATTCCC
ATCCACTTCCCCAAGGATTTCTTGTCTGTGATGCTTGAAAAAGGAAGTTTGTCTGCCATG
CGTTTCCTCACCGCCGTGAACTTGGAGCATCCAGAGATGCTGGAGAAAGCGTCCCGGGAG
CTGTGGATGCGCGTCTGGTCAAGGAATGAAGACATCACCGAGCCGCAGAGCATCCTGGCG
GCTGCAGAGAAGGCTGGTATGTCTGCAGAACAAGCCCAGGGACTTCTGGAAAAGATCGCA
ACGCCAAAGGTGAAGAACCAGCTCAAGGAGACCACTGAGGCAGCCTGCAGATACGGAGCC
TTTGGGCTGCCCATCACCGTGGCCCATGTGGATGGCCAAACCCACATGTTATTTGGCTCT
GACCGGATGGAGCTGCTGGCGCACCTGCTGGGAGAGAAGTGGATGGGCCCTATACCTCCA
GCCGTGAATGCCAGACTTTAA
Enzyme 17 GenBank Gene ID AK289580 Link Image
Enzyme 17 GeneCard ID Q6FII1 Link Image
Enzyme 17 GenAtlas ID LOC51064 Link Image
Enzyme 17 HGNC ID HGNC:16906 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15214
Enzyme 18 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 18 Synonyms Not Available
Enzyme 18 Gene Name MGST1
Enzyme 18 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 18 Number of Residues 155
Enzyme 18 Molecular Weight 17599
Enzyme 18 Theoretical pI 9.71
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158255732 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K533 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K533_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >468 bp
ATGGTTGACCTCACCCAGGTAATGGATGATGAAGTATTCATGGCTTTTGCATCCTATGCA
ACAATTATTCTTTCAAAAATGATGCTTATGAGTACTGCAACTGCATTCTATAGATTGACA
AGAAAGGTTTTTGCCAATCCAGAAGACTGTGTAGCATTTGGCAAAGGTGAAAATGCCAAG
AAGTATCTTCGAACAGATGACAGAGTAGAACGTGTACGCAGAGCCCACCTGAATGACCTT
GAAAATATTATTCCATTTCTTGGAATTGGCCTCCTGTATTCCTTGAGTGGTCCCGACCCC
TCTACAGCCATCCTGCACTTCAGACTATTTGTCGGAGCACGGATCTACCACACCATTGCA
TATTTGACACCCCTTCCCCAGCCAAATAGAGCTTTGAGTTTTTTTGTTGGATATGGAGTT
ACTCTTTCCATGGCTTACAGGTTGCTGAAAAGTAAATTGTACCTGTAA
Enzyme 18 GenBank Gene ID AK291148 Link Image
Enzyme 18 GeneCard ID A8K533 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location 12
Enzyme 18 Locus 12p12.3-p12.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16492
Enzyme 19 Name cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name GSTA4
Enzyme 19 Protein Sequence >cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEI
DGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKE
VVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPF
LQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP
Enzyme 19 Number of Residues 222
Enzyme 19 Molecular Weight 25705
Enzyme 19 Theoretical pI 8.72
Enzyme 19 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 19 General Function Not Available
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID B2RD15 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B2RD15_HUMAN Link Image
Enzyme 19 PDB ID 1GUM Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AK315369 Link Image
Enzyme 19 GeneCard ID B2RD15 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16493
Enzyme 20 Name cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name MGST3
Enzyme 20 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 20 Number of Residues 152
Enzyme 20 Molecular Weight 16516
Enzyme 20 Theoretical pI 9.68
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Not Available
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID B2R592 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name B2R592_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AK312103 Link Image
Enzyme 20 GeneCard ID B2R592 Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References Not Available
Enzyme 20 Metabolite References Not Available