The Enzyme Database

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Accepted name: γ-glutamyl hydrolase
Reaction: Hydrolysis of a γ-glutamyl bond
Other name(s): conjugase; folate conjugase; lysosomal γ-glutamyl carboxypeptidase; γ-Glu-X carboxypeptidase; pteroyl-poly-γ-glutamate hydrolase; carboxypeptidase G; folic acid conjugase; poly(γ-glutamic acid) endohydrolase; polyglutamate hydrolase; poly(glutamic acid) hydrolase II; pteroylpoly-γ-glutamyl hydrolase
Comments: A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Commonly studied with folylpoly-γ-glutamate as substrate, with which the initial cleavage may release glutamate or poly-γ-glutamate of two or more residues, according to the species of origin of the enzyme. Final products are pteroyl-α-glutamate (folic acid) and free glutamate. Highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid (leaving group). Action on γ-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal γ-Glu residue can be hydrolysed. Type example of peptidase family C26.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
1.  McGuire, J.J. and Coward, J.K. Pteroylpolyglutamates: biosynthesis, degradation and function.. In: Blakley, R.L. and Benkovic, S.J. (Eds), Folates and Pterins, John Wiley and Sons, New York, 1984, pp. 135–191.
2.  Wang, Y., Nimec, Z., Ryan, T.J., Dias, J.A. and Galivan, J. The properties of the secreted γ-glutamyl hydrolases from H35 hepatoma cells. Biochim. Biophys. Acta 1164 (1993) 227–235. [PMID: 8343522]
3.  Yao, R., Rhee, M.S. and Galivan, J. Effects of γ-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells. Mol. Pharmacol. 48 (1995) 505–511. [PMID: 7565632]
4.  Yao, R., Schneider, E., Ryan, T.J. and Galivan, J. Human γ-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro. Proc. Natl. Acad. Sci. USA 93 (1996) 10134–10138. [PMID: 8816764]
5.  Yao, R., Nimec, Z., Ryan, T.J. and Galivan, J. Identification, cloning, and sequencing of a cDNA coding for rat γ-glutamyl hydrolase. J. Biol. Chem. 271 (1996) 8525–8528. [PMID: 8621474]
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