Glutamate carboxypeptidase

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Glutamate carboxypeptidase
Identifiers
EC number 3.4.17.11
CAS number 9074-87-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Glutamate carboxypeptidase (EC 3.4.17.11, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups

This zinc enzyme is produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp.

See also[edit]

References[edit]

  1. ^ Goldman, P.; Levy, C.C. (1967). "Carboxypeptidase G: purification and properties". Proc. Natl. Acad. Sci. USA. 58: 1299–1306. doi:10.1073/pnas.58.4.1299. PMC 223923Freely accessible. PMID 5237864. 
  2. ^ McCullogh, J.L.; Chabner, B.A.; Bertino, J.R. (1971). "Purification and properties of carboxypeptidase G1". J. Biol. Chem. 246: 7207–7213. PMID 5129727. 
  3. ^ Albrecht, A.M.; Boldizar, E.; Hutchinson, D.J. (1978). "Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin". J. Bacteriol. 134: 506–513. PMC 222280Freely accessible. PMID 26657. 
  4. ^ Sherwood, R.F.; Melton, R.G.; Alwan, S.A. (1985). "Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16". Eur. J. Biochem. 148: 447–453. doi:10.1111/j.1432-1033.1985.tb08860.x. PMID 3838935. 

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