EC 3.4.17.13 - Muramoyltetrapeptide carboxypeptidase

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IntEnz Enzyme Nomenclature
EC 3.4.17.13

Names

Accepted name:
muramoyltetrapeptide carboxypeptidase
Other names:
L-lysyl-D-alanine carboxypeptidase
LD-carboxypeptidase
carboxypeptidase II
carboxypeptidase IIW
lysyl-D-alanine carboxypeptidase
Systematic name:
-

Reaction

Comments:

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
CAS Registry Number: 60063-80-1
UniProtKB/Swiss-Prot:

References

  1. DasGupta, H. and Fan, D.P.
    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]
  2. Rousset, A., Nguyen-Disteche, M., Minck, R. and Ghuysen, J.-M.
    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]
  3. Metz, R., Henning, S. and Hammes, W.P.
    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 3.4.17.13 created 1992]