Glutamate carboxypeptidase

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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
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MetaCycmetabolic pathway
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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

  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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