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 Gamma-Glutamylcysteine (HMDB01049)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-20 10:48:30
Accession Number HMDB01049
Secondary Accession Numbers Not Available
Common Name Gamma-Glutamylcysteine
Description G-Glutamylcysteine is a product of enzyme glutamate-cysteine ligase [EC 6.3.2.2] and a substrate of enzyme glutathione synthase [EC 6.3.2.3] in glutamate metabolism pathway (KEGG).
Synonyms
  1. (Des-Gly)-Glutathione
  2. 3GC
  3. 5-L-Glutamyl-L-cysteine
  4. H-Glu(Cys-OH)-OH
  5. H-gamma-Glu-Cys-OH
  6. L-g-Glutamyl-L-cysteine
  7. L-gamma-Glutamylcysteine
  8. N-(1-carboxy-2-mercaptoethyl)-L-Glutamine
  9. N-L-gamma-glutamyl-L-Cysteine
  10. g-Glutamylcysteine
  11. g-L-Glutamyl-L-cysteine
  12. gamma-Glu-cys
  13. gamma-Glutamylcysteine
  14. gamma-L-Glutamyl-L-cysteine
  15. xN-L-g-glutamyl-Glutamine
  16. L-gamma-Glutamyl-L-cysteine
  17. xN-L-gamma-glutamyl-Glutamine
  18. 5-L-glutamylcysteine
Chemical IUPAC Name 2-amino-5-(1-carboxy-2-sulfanyl-ethyl)amino-5-oxo-pentanoic acid
Chemical Formula C8H14N2O5S
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 250.272
Monoisotopic Molecular Weight 250.062347
Isomeric SMILES N[C@@H](CCC(=O)N[C@@H](CS)C(O)=O)C(O)=O
Canonical SMILES NC(CCC(=O)NC(CS)C(O)=O)C(O)=O
KEGG Compound ID C00669 Link Image
BioCyc ID L-GAMMA-GLUTAMYLCYSTEINE Link Image
BiGG ID 35655 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01049 Link Image
Metagene Link HMDB01049 Link Image
METLIN ID 5966 Link Image
PubChem Compound 123938 Link Image
PubChem Substance 3938 Link Image
ChEBI ID 17515 Link Image
CAS Registry Number 636-58-8
InChI Identifier InChI=1/C8H14N2O5S/c9-4(7(12)13)1-2-6(11)10-5(3-16)8(14)15/h4-5,16H,1-3,9H2,(H,10,11)(H,12,13)(H,14,15)/t4-,5-/m0/s1
Synthesis Reference Bridge, Wallace John; Zarka, Martin Hani. Enzymic production of g-glutamylcysteine. PCT Int. Appl. (2006), 76pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.62 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.53 [Predicted by ALOGPS]; -5.6 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
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)
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Fibroblasts
Neuron
Concentrations (Normal)
Biofluid Blood
Value 25.0 +/- 8.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 85-97. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 1.9 +/- 0.5 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Andersson A, Isaksson A, Brattstrom L, Hultberg B: Homocysteine and other thiols determined in plasma by HPLC and thiol-specific postcolumn derivatization. Clin Chem. 1993 Aug;39(8):1590-7. [PubMed Link Image]
Biofluid Urine
Value 0.46+/-0.14 umol/mmol creatinine
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Lochman P, Adam T, Friedecky D, Hlidkova E, Skopkova Z: High-throughput capillary electrophoretic method for determination of total aminothiols in plasma and urine. Electrophoresis. 2003 Apr;24(7-8):1200-7. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Cysteine Metabolism SMP00013 Link Image map00270 Link Image
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Glutathione Metabolism SMP00015 Link Image map00480 Link Image
General References
  1. Atamna H, Ginsburg H: The malaria parasite supplies glutathione to its host cell--investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum. Eur J Biochem. 1997 Dec 15;250(3):670-9. [PubMed Link Image]
  2. Efferth T, Volm M: Glutathione-related enzymes contribute to resistance of tumor cells and low toxicity in normal organs to artesunate. In Vivo. 2005 Jan-Feb;19(1):225-32. [PubMed Link Image]
  3. Lochman P, Adam T, Friedecky D, Hlidkova E, Skopkova Z: High-throughput capillary electrophoretic method for determination of total aminothiols in plasma and urine. Electrophoresis. 2003 Apr;24(7-8):1200-7. [PubMed Link Image]
  4. Martensson J: Method for determination of free and total glutathione and gamma-glutamylcysteine concentrations in human leukocytes and plasma. J Chromatogr. 1987 Sep 4;420(1):152-7. [PubMed Link Image]
  5. Andersson A, Isaksson A, Hultberg B: Homocysteine export from erythrocytes and its implication for plasma sampling. Clin Chem. 1992 Jul;38(7):1311-5. [PubMed Link Image]
  6. Kaarteenaho-Wiik R, Kinnula VL: Distribution of antioxidant enzymes in developing human lung, respiratory distress syndrome, and bronchopulmonary dysplasia. J Histochem Cytochem. 2004 Sep;52(9):1231-40. [PubMed Link Image]
  7. 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]
  8. Andersson A, Isaksson A, Brattstrom L, Hultberg B: Homocysteine and other thiols determined in plasma by HPLC and thiol-specific postcolumn derivatization. Clin Chem. 1993 Aug;39(8):1590-7. [PubMed Link Image]
  9. Diaz-Hernandez JI, Almeida A, Delgado-Esteban M, Fernandez E, Bolanos JP: Knockdown of glutamate-cysteine ligase by small hairpin RNA reveals that both catalytic and modulatory subunits are essential for the survival of primary neurons. J Biol Chem. 2005 Nov 25;280(47):38992-9001. Epub 2005 Sep 23. [PubMed Link Image]
  10. Levonen AL, Lapatto R, Saksela M, Raivio KO: Expression of gamma-glutamylcysteine synthetase during development. Pediatr Res. 2000 Feb;47(2):266-70. [PubMed Link Image]
  11. Martensson J, Kagedal B, Larsson A: Sulphur amino-acid degradation in subjects with hereditary glutathione synthetase deficiency (5-oxoprolinuria). Eur J Clin Invest. 1985 Dec;15(6):371-4. [PubMed Link Image]
  12. Zinellu A, Sotgia S, Posadino AM, Pasciu V, Perino MG, Tadolini B, Deiana L, Carru C: Highly sensitive simultaneous detection of cultured cellular thiols by laser induced fluorescence-capillary electrophoresis. Electrophoresis. 2005 Mar;26(6):1063-70. [PubMed Link Image]
  13. Njalsson R, Ristoff E, Carlsson K, Winkler A, Larsson A, Norgren S: Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency. Hum Genet. 2005 Apr;116(5):384-9. Epub 2005 Feb 17. [PubMed Link Image]
  14. Lou MF, Dickerson JE Jr, Tung WH, Wolfe JK, Chylack LT Jr: Correlation of nuclear color and opalescence with protein S-thiolation in human lenses. Exp Eye Res. 1999 May;68(5):547-52. [PubMed Link Image]
Metabolic Enzymes
  1. Glutamate--cysteine ligase catalytic subunit
  2. Glutaminyl-peptide cyclotransferase precursor
  3. Glutathione synthetase
  4. Gamma-glutamylcyclotransferase
Enzyme 1 [top]
Enzyme 1 ID 5759
Enzyme 1 Name Glutamate--cysteine ligase catalytic subunit
Enzyme 1 Synonyms
  1. Gamma- glutamylcysteine synthetase
  2. Gamma-ECS
  3. GCS heavy chain
Enzyme 1 Gene Name GCLC
Enzyme 1 Protein Sequence >Glutamate--cysteine ligase catalytic subunit
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
Enzyme 1 Number of Residues 637
Enzyme 1 Molecular Weight 72767
Enzyme 1 Theoretical pI 5.98
Enzyme 1 GO Classification
Function
  • acid-amino acid ligase activity
  • catalytic activity
  • glutamate-cysteine ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • glutathione biosynthesis
  • glutathione metabolism
  • metabolism
  • physiological process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 183039 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P48506 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GSH1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1914 bp
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
Enzyme 1 GenBank Gene ID M90656 Link Image
Enzyme 1 GeneCard ID GCLC Link Image
Enzyme 1 GenAtlas ID GCLC Link Image
Enzyme 1 HGNC ID HGNC:4311 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [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]
  3. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed Link Image]
  4. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed Link Image]
  5. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5965
Enzyme 2 Name Glutaminyl-peptide cyclotransferase precursor
Enzyme 2 Synonyms
  1. QC
  2. Glutaminyl-tRNA cyclotransferase
  3. Glutaminyl cyclase
Enzyme 2 Gene Name QPCT
Enzyme 2 Protein Sequence >Glutaminyl-peptide cyclotransferase precursor
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGT
SISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSF
SNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLS
LKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG
MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYG
GVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLH
L
Enzyme 2 Number of Residues 361
Enzyme 2 Molecular Weight 40877
Enzyme 2 Theoretical pI 6.60
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • peptidase activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-28
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 296949 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q16769 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name QPCT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1086 bp
ATGGCAGGCGGAAGACACCGGCGCGTCGTGGGCACCCTCCACCTGCTGCTGCTGGTGGCC
GCCCTGCCCTGGGCATCCAGGGGGGTCAGTCCGAGTGCCTCAGCCTGGCCAGAGGAGAAG
AATTACCACCAGCCAGCCATTTTGAATTCATCGGCTCTTCGGCAAATTGCAGAAGGCACC
AGTATCTCTGAAATGTGGCAAAATGACTTACAGCCATTGCTGATAGAGCGATACCCGGGA
TCCCCTGGAAGCTATGCTGCTCGTCAGCACATCATGCAGCGAATTCAGAGGCTTCAGGCT
GACTGGGTCTTGGAAATAGACACCTTCTTGAGTCAGACACCCTATGGGTACCGGTCTTTC
TCAAATATCATCAGCACCCTCAATCCCACTGCTAAACGACATTTGGTCCTCGCCTGCCAC
TATGACTCCAAGTATTTTTCCCACTGGAACAACAGAGTGTTTGTAGGAGCCACTGATTCA
GCCGTGCCATGTGCAATGATGTTGGAACTTGCTCGTGCCTTAGACAAGAAACTCCTTTCC
TTAAAGACTGTTTCAGACTCCAAGCCAGATTTGTCACTCCAGCTGATCTTCTTTGATGGT
GAAGAGGCTTTTCTTCACTGGTCTCCTCAAGATTCTCTCTATGGGTCTCGACACTTAGCT
GCAAAGATGGCATCGACCCCGCACCCACCTGGAGCGAGAGGCACCAGCCAACTGCATGGC
ATGGATTTATTGGTCTTATTGGATTTGATTGGAGCTCCAAACCCAACGTTTCCCAATTTT
TTTCCAAACTCAGCCAGGTGGTTCGAAAGACTTCAAGCAATTGAACATGAACTTCATGAA
TTGGGTTTGCTCAAGGATCACTCTTTGGAGGGGCGGTATTTCCAGAATTACAGTTATGGA
GGTGTGATTCAGGATGACCATATTCCATTTTTAAGAAGAGGTGTTCCAGTTCTGCATCTG
ATACCGTCTCCTTTCCCTGAAGTCTGGCACACCATGGATGACAATGAAGAAAATTTGGAT
GAATCAACCATTGACAATCTAAACAAAATCCTACAAGTCTTTGTGTTGGAATATCTTCAT
TTGTAA
Enzyme 2 GenBank Gene ID X71125 Link Image
Enzyme 2 GeneCard ID QPCT Link Image
Enzyme 2 GenAtlas ID QPCT Link Image
Enzyme 2 HGNC ID HGNC:9753 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p22.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Song I, Chuang CZ, Bateman RC Jr: Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J Mol Endocrinol. 1994 Aug;13(1):77-86. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6071
Enzyme 3 Name Glutathione synthetase
Enzyme 3 Synonyms
  1. Glutathione synthase
  2. GSH synthetase
  3. GSH-S
Enzyme 3 Gene Name GSS
Enzyme 3 Protein Sequence >Glutathione synthetase
MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSA
LLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVF
LGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKIL
SNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFE
DISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQ
LAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSR
FVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVV
QCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV
Enzyme 3 Number of Residues 474
Enzyme 3 Molecular Weight 52385
Enzyme 3 Theoretical pI 5.73
Enzyme 3 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 3 General Function Not Available
Enzyme 3 Specific Function ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + 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 886284 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P48637 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GSHB_HUMAN Link Image
Enzyme 3 PDB ID 2HGS Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID L42531 Link Image
Enzyme 3 GeneCard ID GSS Link Image
Enzyme 3 GenAtlas ID GSS Link Image
Enzyme 3 HGNC ID HGNC:4624 Link Image
Enzyme 3 Chromosome Location 20
Enzyme 3 Locus 20q11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15259
Enzyme 4 Name Gamma-glutamylcyclotransferase
Enzyme 4 Synonyms
  1. Cytochrome c-releasing factor 21
Enzyme 4 Gene Name GGCT
Enzyme 4 Protein Sequence >Gamma-glutamylcyclotransferase
MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKT
SQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEI
TCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDII
KKGETQTL
Enzyme 4 Number of Residues 188
Enzyme 4 Molecular Weight 21008
Enzyme 4 Theoretical pI 4.79
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Catalyzes the formation of 5-oxoproline from gamma- glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 189054993 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75223 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GGCT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >567 bp
ATGGCCAACTCGGGCTGCAAGGACGTCACGGGTCCAGATGAGGAGAGTTTTCTGTACTTT
GCCTACGGCAGCAACCTGCTGACAGAGAGGATCCACCTCCGAAACCCCTCGGCGGCGTTC
TTCTGTGTGGCCCGCCTGCAGGATTTTAAGCTTGACTTTGGCAATTCCCAAGGCAAAACA
AGTCAAACTTGGCATGGAGGGATAGCCACCATTTTTCAGAGTCCTGGCGATGAAGTGTGG
GGAGTAGTATGGAAAATGAACAAAAGCAATTTAAATTCTCTGGATGAGCAAGAAGGGGTT
AAAAGTGGAATGTATGTTGTAATAGAAGTTAAAGTTGCAACTCAAGAAGGAAAAGAAATA
ACCTGTCGAAGTTATCTGATGACAAATTACGAAAGTGCTCCCCCATCCCCACAGTATAAA
AAGATTATTTGCATGGGTGCAAAAGAAAATGGTTTGCCGCTGGAGTATCAAGAGAAGTTA
AAAGCAATAGAACCAAATGACTATACAGGAAAGGTCTCAGAAGAAATTGAAGACATCATC
AAAAAGGGGGAAACACAAACTCTTTAG
Enzyme 4 GenBank Gene ID AK315608 Link Image
Enzyme 4 GeneCard ID O75223 Link Image
Enzyme 4 GenAtlas ID GGCT Link Image
Enzyme 4 HGNC ID HGNC:21705 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available