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Muramoylpentapeptide carboxypeptidase (EC3.4.17.8, D-alanine carboxypeptidase I, DD-carboxypeptidase, D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanine-D-alanine-carboxypeptidase, carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase, D-alanyl-D-alanine peptidase, DD-peptidase, penicillin binding protein 5, PBP5, PdcA, VanY) is an enzyme. This enzyme catalyses the following chemical reaction.
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl--D-alanine
This bacterial enzyme that requires a divalent cation for activity.
References
Izaki K, Strominger JL (June 1968). "Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". The Journal of Biological Chemistry. 243 (11): 3193–201. PMID4871206.