| EC |
3.4.17.8 |
| Accepted name: |
muramoylpentapeptide carboxypeptidase |
| Reaction: |
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanyl┼D-alanine |
| Other name(s): |
D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY |
| Comments: |
A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanine. Competitively inhibited by penicillins and cephalosporins. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9077-67-2 |
| References: |
| 1. |
Izaki, K. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J. Biol. Chem. 243 (1968) 3193–3201. [PMID: 4871206] |
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| [EC 3.4.17.8 created 1972 as EC 3.4.12.6, transferred 1978 to EC 3.4.17.8] |
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