| EC |
3.4.16.4 |
| Accepted name: |
serine-type D-Ala-D-Ala carboxypeptidase |
| Reaction: |
Preferential cleavage: (Ac)2-L-Lys-D-Ala┼D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine |
| Other name(s): |
DD-peptidase; D-alanyl-D-alanine-carboxypeptidase; D-alanyl-D-alanine-cleaving-peptidase; D-alanyl-D-alanine-cleaving peptidase; DD-transpeptidase; D-alanine carboxypeptidase; DD-carboxypeptidase; D-alanyl carboxypeptidase |
| Comments: |
A membrane-bound, bacterial enzyme inhibited by penicillin and other β-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase families S11, S12 and S13. Distinct from EC 3.4.17.14, zinc D-Ala-D-Ala carboxypeptidase |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9077-67-2 |
| References: |
| 1. |
Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J., Dusart, J., Joris, B., Duez, C., Dideberg, O., Charlier, P., Dive, G. and Lamotte-Brasseur, J. Bacterial wall peptidoglycan, DD-peptidases and β-lactam antibiotics. Scand. J. Infect. Dis. Suppl. 42 (1984) 17–37. [PMID: 6597561] |
| 2. |
Frère, J.M. and Joris, B. Penicillin-sensitive enzymes in peptidoglycan biosynthesis. CRC Crit. Rev. Microbiol. 11 (1985) 306–331. [PMID: 3888533] |
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| [EC 3.4.16.4 created 1989] |
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