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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 JM, Ghuysen JM (September 1982). "Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution". Nature. 299 (5882): 469–70. doi:10.1038/299469a0. PMID 7121588.
- ^ Joris B, Van Beeumen J, Casagrande F, Gerday C, Frère JM, Ghuysen JM (January 1983). "The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G". European Journal of Biochemistry. 130 (1): 53–69. doi:10.1111/j.1432-1033.1983.tb07116.x. PMID 6825689.
- ^ Ghuysen JM, Frère JM, Leyh-Bouille M, Nguyen-Distèche M, Coyette J, Dusart J, Joris B, Duez C, Dideberg O, Charlier P (1984). "Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics". Scandinavian Journal of Infectious Diseases. Supplementum. 42: 17–37. PMID 6597561.
External links
- Zinc+D-Ala-D-Ala+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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