Muramoylpentapeptide carboxypeptidase
Muramoylpentapeptide carboxypeptidase (EC 3.4.17.8, 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.[1] 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. and Strominger, J.L. (1968). "Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli". J. Biol. Chem. 243: 3193–3201. PMID 4871206.
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