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
Muramoylpentapeptide carboxypeptidase
Identifiers
EC no.3.4.17.8
CAS no.9077-67-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

This bacterial enzyme that requires a divalent cation for activity.

References

  1. 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. PMID 4871206.
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