Glutamate carboxypeptidase
| 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
References
- ↑ Goldman, P.; Levy, C.C. (1967). "Carboxypeptidase G: purification and properties". Proc. Natl. Acad. Sci. USA. 58: 1299–1306. PMID 5237864.
- ↑ McCullogh, J.L.; Chabner, B.A.; Bertino, J.R. (1971). "Purification and properties of carboxypeptidase G1". J. Biol. Chem. 246: 7207–7213. PMID 5129727.
- ↑ 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. PMID 26657.
- ↑ 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.
External links
- Glutamate carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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