KEGG   ENZYME: 3.4.19.13Help
Entry
EC 3.4.19.13                Enzyme                                 

Name
glutathione hydrolase;
glutathionase;
GGT (ambiguous);
gamma-glutamyltranspeptidase (ambiguous)
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Omega peptidases
BRITE hierarchy
Reaction(IUBMB)
glutathione + H2O = L-cysteinylglycine + L-glutamate [RN:R00494]
Reaction(KEGG)
Substrate
glutathione [CPD:C00051];
H2O [CPD:C00001]
Product
L-cysteinylglycine [CPD:C01419];
L-glutamate [CPD:C00025]
Comment
This protein also has EC 2.3.2.2 (gamma-glutamyltransferase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [2-5]. The human enzyme also hydrolyses oxidized glutathione and leukotriene C4 with similar efficiency, while the mouse enzyme does not [6-7].
History
EC 3.4.19.13 created 2011
Reference
1  [PMID:8099811]
  Authors
Hanigan MH, Ricketts WA
  Title
Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase.
  Journal
Biochemistry. 32 (1993) 6302-6.
Reference
2  [PMID:12207027]
  Authors
Suzuki H, Kumagai H
  Title
Autocatalytic processing of gamma-glutamyltranspeptidase.
  Journal
J. Biol. Chem. 277 (2002) 43536-43.
Reference
3  [PMID:16618936]
  Authors
Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K
  Title
Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 6471-6.
  Sequence
[eco:b3447]
Reference
4  [PMID:17107958]
  Authors
Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ
  Title
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.
  Journal
J. Biol. Chem. 282 (2007) 534-41.
Reference
5  [PMID:17135273]
  Authors
Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K
  Title
Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.
  Journal
J. Biol. Chem. 282 (2007) 2433-9.
  Sequence
[eco:b3447]
Reference
6  [PMID:21447318]
  Authors
Wickham S, West MB, Cook PF, Hanigan MH
  Title
Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase  enzymes.
  Journal
Anal. Biochem. 414 (2011) 208-14.
Reference
7  [PMID:9139674]
  Authors
Carter BZ, Wiseman AL, Orkiszewski R, Ballard KD, Ou CN, Lieberman MW
  Title
Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice.
  Journal
J. Biol. Chem. 272 (1997) 12305-10.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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