EC 3 - Hydrolases
EC 3.4 - Acting on peptide bonds (peptidases)
EC 3.4.16 - Serine-type carboxypeptidases
EC 3.4.16.4 - Serine-type D-Ala-D-Ala carboxypeptidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.4.16.4
Names
Accepted name:
serine-type D-Ala-D-Ala carboxypeptidase
Other
names:
D-alanine carboxypeptidase
D-alanyl carboxypeptidase
D-alanyl-D-alanine-carboxypeptidase
D-alanyl-D-alanine-cleaving peptidase
D-alanyl-D-alanine-cleaving-peptidase
DD-carboxypeptidase
DD-peptidase
DD-transpeptidase
D-alanyl-D-alanine carboxypeptidase
D-alanyl carboxypeptidase
D-alanyl-D-alanine-carboxypeptidase
D-alanyl-D-alanine-cleaving peptidase
D-alanyl-D-alanine-cleaving-peptidase
DD-carboxypeptidase
DD-peptidase
DD-transpeptidase
D-alanyl-D-alanine carboxypeptidase
Systematic name:
-
Reaction
- Preferential cleavage: (Ac)2-L-Lys-D-AlaD-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
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 zinc D-Ala-D-Ala carboxypeptidase, EC 3.4.17.14.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
MEROPS
,
MEROPS
,
MEROPS
,
UniPathway
Gene Ontology:
GO:0009002
CAS Registry Number:
9077-67-2
References
-
Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics.Scand. J. Infect. Dis. 42 : 17-37 (1984). [PMID: 6597561]
-
Penicillin-sensitive enzymes in peptidoglycan biosynthesis.CRC Crit. Rev. Microbiol. 11 : 306-331 (1985). [PMID: 3888533]
[EC 3.4.16.4 created 1989]