Enzyme

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     3. Hydrolases
        3.4 Acting on peptide bonds (peptidases)
            3.4.19 Omega peptidases
ID:3.4.19.13
Description:Glutathione gamma-glutamate hydrolase.
Alternative Name: Glutathionase.
Gamma-glutamyltranspeptidase.
Cath: 1.10.246.130; 3.60.20.40;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.4.19.13
BRENDA Enzyme Link: BRENDA 3.4.19.13
KEGG Enzyme Link: KEGG3.4.19.13
BioCyc Enzyme Link: BioCyc 3.4.19.13
ExPASy Enzyme Link: ExPASy3.4.19.13
EC2PDB Enzyme Link: EC2PDB 3.4.19.13
ExplorEnz Enzyme Link: ExplorEnz 3.4.19.13
PRIAM enzyme-specific profiles Link: PRIAM 3.4.19.13
IntEnz Enzyme Link: IntEnz 3.4.19.13
MEDLINE Enzyme Link: MEDLINE 3.4.19.13
MSA:

3.4.19.13;

Phylogenetic Tree:

3.4.19.13;

Uniprot:
M-CSA:
RHEA:28807 glutathione + H2O = L-cysteinylglycine + L-glutamate
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis.Grzam A, Martin MN, Hell R, Meyer AJ2007 Jul 1017561001
Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K2007 Jan 2617135273
Autocatalytic processing of gamma-glutamyltranspeptidase.Suzuki H, Kumagai H2002 Nov 812207027
Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential.Suzuki H, Hashimoto W, Kumagai H1993 Sep8104180
Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase.Hanigan MH, Ricketts WA1993 Jun 228099811
Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes.Wickham S, West MB, Cook PF, Hanigan MH2011 Jul 1521447318
Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K2006 Apr 2516618936