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Information on EC 3.4.19.9 - folate gamma-glutamyl hydrolase

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.19 Omega peptidases
                3.4.19.9 folate gamma-glutamyl hydrolase
IUBMB Comments
A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH. Commonly studied with folylpoly-gamma-glutamate as substrate, with which the initial cleavage may release glutamate or poly-gamma-glutamate of two or more residues, according to the species of origin of the enzyme. Final products are pteroyl-alpha-glutamate (folic acid) and free glutamate. Highly specific for the gamma-glutamyl bond, but not for the C-terminal amino acid (leaving group). Action on gamma-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it is not known whether an N-terminal gamma-Glu residue can be hydrolysed. Type example of peptidase family C26.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
tetrahydropteroyl-(gamma-glutamyl)n
+
(n-1)
=
+
(n-1)
Synonyms
conjugase, folate hydrolase, folate conjugase, folylpolyglutamate hydrolase, gamma-gh, leggh2, leggh3, zgammagh, leggh1, low gamma-glutamyl hydrolase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tetrahydropteroyl-(gamma-glutamyl)n + (n-1) H2O = 5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
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PATHWAY SOURCE
PATHWAYS
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