Glutamate carboxypeptidase

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
Glutamate carboxypeptidase
Space-filling model of Pseudomonas carboxypeptidase G2, expressed in Escherichia coli. PDB: 1CG2.
Identifiers
EC no.3.4.17.11
CAS no.9074-87-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

See also

References

  1. Goldman P, Levy CC (October 1967). "Carboxypeptidase G: purification and properties". Proceedings of the National Academy of Sciences of the United States of America. 58 (4): 1299–306. Bibcode:1967PNAS...58.1299G. doi:10.1073/pnas.58.4.1299. PMC 223923. PMID 5237864.
  2. McCullough JL, Chabner BA, Bertino JR (December 1971). "Purification and properties of carboxypeptidase G 1". The Journal of Biological Chemistry. 246 (23): 7207–13. doi:10.1016/S0021-9258(19)45873-0. PMID 5129727.
  3. Albrecht AM, Boldizsar E, Hutchison DJ (May 1978). "Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin". Journal of Bacteriology. 134 (2): 506–13. doi:10.1128/jb.134.2.506-513.1978. PMC 222280. PMID 26657.
  4. Sherwood RF, Melton RG, Alwan SM, Hughes P (May 1985). "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. doi:10.1111/j.1432-1033.1985.tb08860.x. PMID 3838935.
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