Muramoyltetrapeptide carboxypeptidase
| Muramoyltetrapeptide carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.13 | ||||||||
| CAS no. | 60063-80-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Muramoyltetrapeptide carboxypeptidase (EC 3.4.17.13, carboxypeptidase IIW, carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl--D-alanine
Variants are known from various microorganisms.
References
- ^ DasGupta, H.; Fan, D.P. (1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan". J. Biol. Chem. 254: 5672–5683. PMID 109439.
- ^ Rousset, A.; Nguyen-Disteche, M.; Minck, R.; Ghuysen, J.-M. (1982). "Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms". J. Bacteriol. 152: 1042–1048. PMC 221607. PMID 6754695.
- ^ Metz, R.; Henning, S.; Hammes, W.P. (1986). "LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12". Arch. Microbiol. 144: 181–186. doi:10.1007/bf00414732. PMID 3521530.
External links
- Muramoyltetrapeptide+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)