EC 22.214.171.124 - Muramoyltetrapeptide carboxypeptidase
IntEnz Enzyme Nomenclature
- Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysylD-alanine.
Variants are known from various microorganisms. Involved in peptidoglycan synthesis, catalysing both decarboxylation and transpeptidation. Stimulated by divalent cations such as Mg2+ and Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but unaffected by penicillin.
Links to other databases
Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan.J. Biol. Chem. 254 : 5672-5683 (1979). [PMID: 109439]
Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms.J. Bacteriol. 152 : 1042-1048 (1982). [PMID: 6754695]
LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12.Arch. Microbiol. 144 : 181-186 (1986).
[EC 126.96.36.199 created 1992]