EC 2.3.2.2 - γ-glutamyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.2.2

Names

Accepted name:
γ-glutamyltransferase
Other names:
α-glutamyl transpeptidase
γ-GPT
γ-GT
γ-GTP
γ-glutamyl peptidyltransferase
γ-glutamyl transpeptidase [ambiguous]
L-γ-glutamyl transpeptidase
L-γ-glutamyltransferase
L-glutamyltransferase
glutamyl transpeptidase
GGT [ambiguous]
γ-glutamyltranspeptidase [ambiguous]
Systematic name:
(5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase

Reaction

Comments:

The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. 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 [3-4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00404
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003840
CAS Registry Number: 9046-27-9
UniProtKB/Swiss-Prot: (32) [show] [UniProt]

References

  1. Goore, M.Y. and Thompson, J.F.
    γ-Glutamyl transpeptidase from kidney bean fruit. I. Purification and mechanism of action.
    Biochim. Biophys. Acta 132: 15-26 (1967). [PMID: 6030345]
  2. Leibach, F.H. and Binkley, F.
    γ-Glutamyl transferase of swine kidney.
    Arch. Biochem. Biophys. 127: 292-301 (1968). [PMID: 5698023]
  3. Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K.
    Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
    Proc. Natl. Acad. Sci. U.S.A. 103: 6471-6476 (2006). [PMID: 16618936]
  4. Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K., Barycki, J. J.
    Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.
    J. Biol. Chem. 282: 534-541 (2007). [PMID: 17107958]
  5. Wickham, S., West, M. B., Cook, P. F., Hanigan, M. H.
    Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes.
    Anal. Biochem. 414: 208-214 (2011). [PMID: 21447318]

[EC 2.3.2.2 created 1972, modified 1976, modified 2011]