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Glutamate carboxypeptidase
| Field | Value |
|---|---|
| Name | Glutamate carboxypeptidase |
| EC_number | 3.4.17.11 |
| CAS_number | 9074-87-7 |
| image | Glutamate carboxypeptidase 1CG2.png |
| caption | Space-filling model of Pseudomonas carboxypeptidase G2, expressed in Escherichia coli. . |
Glutamate carboxypeptidase (, carboxypeptidase G, carboxypeptidase G1, carboxypeptidase G2, glutamyl carboxypeptidase, N-pteroyl-L-glutamate hydrolase) is an enzyme. 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.
References
References
- (October 1967). "Carboxypeptidase G: purification and properties". Proceedings of the National Academy of Sciences of the United States of America.
- (December 1971). "Purification and properties of carboxypeptidase G 1". The Journal of Biological Chemistry.
- (May 1978). "Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin". Journal of Bacteriology.
- (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.
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