EC 18.104.22.168 - γ-glutamyl hydrolase
IntEnz Enzyme Nomenclature
folic acid conjugase
lysosomal γ-glutamyl carboxypeptidase
poly(γ-glutamic acid) endohydrolase
poly(glutamic acid) hydrolase II
- Hydrolysis of a γ-glutamyl bond.
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. Formerly EC 22.214.171.124.
Links to other databases
Pteroylpolyglutamates: biosynthesis, degradation and function.In: Blakley, R.L. and Benkovic, S.J. (Eds.) Folates and Pterins, John Wiley and Sons, New York, 1984, 135-191
The properties of the secreted γ-glutamyl hydrolases from H35 hepatoma cells.Biochim. Biophys. Acta 1164: 227-235 (1993). [PMID: 8343522]
Effects of γ-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells.Mol. Pharmacol. 48: 505-511 (1995). [PMID: 7565632]
Human γ-glutamyl hydrolase: Cloning and characterization of the enzyme expressed in vitro.Proc. Natl. Acad. Sci. USA 93: 10134-10138 (1996). [PMID: 8816764]
Identification, cloning, and sequencing of a cDNA coding for rat γ-glutamyl hydrolase.J. Biol. Chem. 271: 8525-8528 (1996). [PMID: 8621474]
[EC 126.96.36.199 created 1972 as EC 188.8.131.52, transferred 1978 to EC 184.108.40.206, transferred 1992 to EC 220.127.116.11, modified 1997]