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Your query returned 1 entry. Printable version
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 | ||||
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