EC 3.4.16.4: Serine-type D-Ala-D-Ala carboxypeptidase
Reaction catalysed:
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Systematic name:
-
Alternative Name(s):
- D-alanine carboxypeptidase
- D-alanyl carboxypeptidase
- D-alanyl-D-alanine carboxypeptidase
- D-alanyl-D-alanine-carboxypeptidase
- D-alanyl-D-alanine-cleaving peptidase
- D-alanyl-D-alanine-cleaving-peptidase
- DD-carboxypeptidase
- DD-peptidase
- DD-transpeptidase
GO terms
Biochemical function:
Biological process:
Cellular component:
Sequence families
Protein families (Pfam)
InterPro annotations
IPR037167
Domain description:
D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily
Occurring in:
Occurring in:
IPR015956
Domain description:
Penicillin-binding protein, C-terminal domain superfamily
Occurring in:
Occurring in:
IPR012907
Domain description:
Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal
Occurring in:
Occurring in:
Structure domains
CATH domains
2.60.410.10
Class:
Mainly Beta
Architecture:
Sandwich
Topology:
Peptidoglycan synthesis regulatory factor (PBP3), Domain 2
Homology:
D-Ala-D-Ala carboxypeptidase, C-terminal domain
Occurring in: