ENTRY       EC 3.4.19.9
NAME        gamma-Glu-X carboxypeptidase
            Conjugase
            Folate conjugase
            Pteroyl-poly-gamma-glutamate hydrolase
            Carboxypeptidase G
            gamma-Glutamyl hydrolase
            Lysosomal gamma-glutamyl carboxypeptidase
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Omega peptidases
REACTION    Cleavage of a gamma-glutamyl bond to release an unsubstituted
            C-terminal amino acid
SUBSTRATE   Peptide
            H2O
            Pteroylpoly-gamma-glutamate
PRODUCT     Amino acid
            Peptide
            Folic acid
COMMENT     A lysosomal, thiol-dependent carboxypeptidase that progressively
            removes gamma-glutamyl residues at acidic pH from pteroylpoly-
            gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and
            free glutamic acid. The presence of a free alpha-carboxyl group
            at each gamma-glutamyl linkage in a polyp-gamma-glutamate chain
            may account for reports that more than one gamma-glutamyl residue
            may be released at a time. Highly specific for gamma-glutamyl
            bond, but not for the C-terminal amino acid (leaving group).
            Action on gamma-glutamyl bonds is independent on an N-terminal
            pteroyl moiety.  Formerly EC 3.4.22.12.
PATHWAY     PATH: MAP00790  Folate biosynthesis
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.19.9
            WIT (What Is There) Metabolic Reconstruction: 3.4.19.9
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