The Enzyme Database

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EC 3.4.17.21     
Accepted name: glutamate carboxypeptidase II
Reaction: Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-γ-glutamates
Glossary: quisqualic acid = 3-(3,5-dioxo-1,2,4-oxazadiazolidin-2-yl)Ala
Other name(s): N-acetylated-γ-linked-acidic dipeptidase (NAALADase); folate hydrolase; prostate-specific membrane antigen; pteroylpoly-γ-glutamate carboxypeptidase; microsomal γ-glutamyl carboxypeptidase; pteroylpolyglutamate hydrolase; folylpolyglutamate hydrolase; pteroylpoly-γ-glutamate hydrolase; pteroylpolygammaglutamyl hydrolase; pteroylpolyglutamic acid hydrolase; PSM antigen; acetylaspartylglutamate dipeptidase; NAALA dipeptidase; rat NAAG peptidase; mGCP; membrane glutamate carboxypeptidase; N-acetylated-α-linked-amino dipeptidase; prostrate-specific membrane antigen; N-Acetylated α-linked acidic dipeptidase; PSMA
Comments: A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa , but also exists in a soluble form. Hydrolyses α-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also γ-glutamyl bonds in γ-Glu-Glu, and folylpoly-γ-glutamates. With folylpoly-γ-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate [4]. Does not hydrolyse Ac-β-Asp-Glu. Known inhibitors: quisqualic acid, Ac-β-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. The release of C-terminal glutamate from folylpoly-γ-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (folate γ-glutamyl hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Heston, W.D.W. Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase. Urology 49 (1997) 104–112. [PMID: 9123729]
2.  Rawlings, N.D. and Barrett, A.J. Structure of membrane glutamate carboxypeptidase. Biochim. Biophys. Acta 1339 (1997) 247–252. [DOI] [PMID: 9187245]
3.  Halsted, C.H., Ling, E.-H., Luthi-Carter, R., Villanueva, J.A., Gardner, J.M., Coyle, J.T. Folylpoly-γ-glutamate carboxypeptidase from pig jejunum: molecular characterization and relation to glutamate carboxypeptidase II. J. Biol. Chem. 273 (1998) 20417–20424. [DOI] [PMID: 9685395]
4.  Luthi-Carter, R., Berger, U.V., Barczak, A.K., Enna, M. and Coyle, J.T. Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II. Proc. Natl. Acad. Sci. USA 95 (1998) 3215–3220. [DOI] [PMID: 9501243]
[EC 3.4.17.21 created 1997, modified 2000 (EC 3.4.13.8 created 1972 and EC 3.4.19.8 created 1992, incorporated 2000)]
 
 


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