Biology:Glutamate carboxypeptidase
From HandWiki
| Glutamate carboxypeptidase | |||||||||
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| 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 | ||||||||
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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
- ↑ "Carboxypeptidase G: purification and properties". Proceedings of the National Academy of Sciences of the United States of America 58 (4): 1299–306. October 1967. doi:10.1073/pnas.58.4.1299. PMID 5237864. Bibcode: 1967PNAS...58.1299G.
- ↑ "Purification and properties of carboxypeptidase G 1". The Journal of Biological Chemistry 246 (23): 7207–13. December 1971. doi:10.1016/S0021-9258(19)45873-0. PMID 5129727.
- ↑ "Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin". Journal of Bacteriology 134 (2): 506–13. May 1978. doi:10.1128/jb.134.2.506-513.1978. PMID 26657.
- ↑ "Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method". European Journal of Biochemistry 148 (3): 447–53. May 1985. 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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