Biology:Muramoyltetrapeptide carboxypeptidase
From HandWiki
| Muramoyltetrapeptide carboxypeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.17.13 | ||||||||
| CAS number | 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 | ||||||||
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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
- ↑ "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan". The Journal of Biological Chemistry 254 (13): 5672–83. July 1979. PMID 109439.
- ↑ "Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms". Journal of Bacteriology 152 (3): 1042–8. December 1982. PMID 6754695.
- ↑ "LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12". Archives of Microbiology 144 (2): 181–6. March 1986. doi:10.1007/bf00414732. PMID 3521530.
External links
- Muramoyltetrapeptide+carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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