ENZYME entry: EC 3.4.19.9

Accepted Name
Gamma-glutamyl hydrolase.
Alternative Name(s)
Carboxypeptidase G.
Conjugase.
Folate conjugase.
Gamma-Glu-X carboxypeptidase.
Lysosomal gamma-glutamyl carboxypeptidase.
Pteroyl-poly-alpha-glutamate hydrolase.
Reaction catalysed
Hydrolysis of a gamma-glutamyl bond
Comment(s)
  • 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 hydrolyzed.
  • Belongs to peptidase family C26.
  • Formerly EC 3.4.12.10 and EC 3.4.22.12.
Cross-references
PROSITEPDOC51275
BRENDA3.4.19.9
EC2PDB3.4.19.9
ExplorEnz3.4.19.9
PRIAM enzyme-specific profiles3.4.19.9
KEGG Ligand Database for Enzyme Nomenclature3.4.19.9
IUBMB Enzyme Nomenclature3.4.19.9
IntEnz3.4.19.9
MEDLINEFind literature relating to 3.4.19.9
MetaCyc3.4.19.9
UniProtKB/Swiss-Prot
Q9SYL6, GGH1_ARATH;  O65355, GGH2_ARATH;  Q9ZV85, GGH3_ARATH;  
Q54LN4, GGHA_DICDI;  Q54HL4, GGHB_DICDI;  A7YWG4, GGH_BOVIN;  
Q92820, GGH_HUMAN;  Q9Z0L8, GGH_MOUSE;  Q62867, GGH_RAT;  
P93164, GGH_SOYBN;  

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