Zinc D-Ala-D-Ala carboxypeptidase
| Zinc D-Ala-D-Ala carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.14 | ||||||||
| CAS number | 213189-85-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14, Zn2+ G peptidase, D-alanyl-D-alanine hydrolase, D-alanyl-D-alanine-cleaving carboxypeptidase, DD-carboxypeptidase, G enzyme, DD-carboxypeptidase-transpeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl--D-alanine
This is a zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism.
References
- ↑ Dideberg, O.; Charlier, P.; Dive, G.; Joris, B.; Frère, J.M.; Ghuysen, J.M. (1982). "Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution". Nature. 299 (5882): 469–470. doi:10.1038/299469a0. PMID 7121588.
- ↑ Joris, B.; Van Beeumen, J.; Casagrande, F.; Gerday, C.; Frère, J.-M.; Ghuysen, J.-M. (1983). "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G". Eur. J. Biochem. 130 (1): 53–69. doi:10.1111/j.1432-1033.1983.tb07116.x. PMID 6825689.
- ↑ Ghuysen, J.-M.; Frère, J.-M.; Leyh-Bouille, M.; Nguyen-Distèche, M.; Coyette, J.; Dusart, J.; Joris, B.; Duez, C.; Dideberg, O.; Charlier, P.; Dive, G.; Lamotte-Brasseur, J. (1984). "Bacterial wall peptidoglycan, DD-peptidases and β-lactam antibiotics". Scand. J. Infect. Dis. Suppl. 42: 17–37. PMID 6597561.
External links
- Zinc D-Ala-D-Ala carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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