The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.4.17.11     
Accepted name: glutamate carboxypeptidase
Reaction: Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups
Other name(s): carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase
Comments: A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Goldman, P. and Levy, C.C. Carboxypeptidase G: purification and properties. Proc. Natl Acad. Sci. USA 58 (1967) 1299–1306. [PMID: 5237864]
2.  McCullogh, J.L., Chabner, B.A. and Bertino, J.R. Purification and properties of carboxypeptidase G1. J. Biol. Chem. 246 (1971) 7207–7213. [PMID: 5129727]
3.  Albrecht, A.M., Boldizar, E. and Hutchinson, D.J. Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin. J. Bacteriol. 134 (1978) 506–513. [PMID: 26657]
4.  Sherwood, R.F., Melton, R.G. and Alwan, S.A. Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Eur. J. Biochem. 148 (1985) 447–453. [PMID: 3838935]
[EC 3.4.17.11 created 1992]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald