| EC |
3.4.17.13 |
| Accepted name: |
muramoyltetrapeptide carboxypeptidase |
| Reaction: |
Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl┼D-alanine |
| Other name(s): |
carboxypeptidase IIW; carboxypeptidase II; lysyl-D-alanine carboxypeptidase; L-lysyl-D-alanine carboxypeptidase; LD-carboxypeptidase |
| 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-80-1 |
| 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 (1979) 5672–5683. [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 (1982) 1042–1048. [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 (1986) 181–186. [PMID: 3521530] |
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| [EC 3.4.17.13 created 1992] |
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