EC 3.4.19.13 - Glutathione hydrolase

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IntEnz Enzyme Nomenclature
EC 3.4.19.13

Names

Accepted name:
glutathione hydrolase
Other names:
glutathionase
GGT [ambiguous]
γ-glutamyltranspeptidase [ambiguous]
Systematic name:
-

Reaction

Comments:

This protein also has EC 2.3.2.2 (γ-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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0036374
UniProtKB/Swiss-Prot: (33) [show] [UniProt]

References

  1. Hanigan, M. H., Ricketts, W. A.
    Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase.
    Biochemistry 32: 6302-6306 (1993). [PMID: 8099811]
  2. Suzuki, H., Kumagai, H.
    Autocatalytic processing of gamma-glutamyltranspeptidase.
    J. Biol. Chem. 277: 43536-43543 (2002). [PMID: 12207027]
  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. Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K.
    Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.
    J. Biol. Chem. 282: 2433-2439 (2007). [PMID: 17135273]
  6. 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]
  7. Carter, B. Z., Wiseman, A. L., Orkiszewski, R., Ballard, K. D., Ou, C. N., Lieberman, M. W.
    Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice.
    J. Biol. Chem. 272: 12305-12310 (1997). [PMID: 9139674]

[EC 3.4.19.13 created 2011]