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

  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. 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. 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. 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.