Muramoylpentapeptide carboxypeptidase explained

Muramoylpentapeptide carboxypeptidase
Ec Number:3.4.17.8
Cas Number:9077-67-2

Muramoylpentapeptide carboxypeptidase (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.

Notes and References

  1. Izaki K, Strominger JL . 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 . June 1968 . 4871206 .