ENZYME entry: EC 3.4.17.8

Accepted Name
Muramoylpentapeptide carboxypeptidase.
Alternative Name(s)
Carboxypeptidase D-alanyl-D-alanine.
D-alanine carboxypeptidase.
D-alanine-D-alanine-carboxypeptidase.
D-alanyl-D-alanine carboxypeptidase.
D-alanyl-D-alanine peptidase.
DD-carboxypeptidase.
DD-peptidase.
PBP5.
Penicillin binding protein 5.
UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase.
Reaction catalysed
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-|-D-alanine
Cofactor(s)
Zn(2+).
Comment(s)
  • Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-D-gamma-glutamyl-6- carboxy-L-lysyl-D-alanine.
  • Competitively inhibited by penicillins and cephalosporins.
  • Belongs to peptidase family M15.
  • Formerly EC 3.4.12.6.
Cross-references
BRENDA3.4.17.8
EC2PDB3.4.17.8
ExplorEnz3.4.17.8
PRIAM enzyme-specific profiles3.4.17.8
KEGG Ligand Database for Enzyme Nomenclature3.4.17.8
IUBMB Enzyme Nomenclature3.4.17.8
IntEnz3.4.17.8
MEDLINEFind literature relating to 3.4.17.8
MetaCyc3.4.17.8

View entry in original ENZYME format
View entry in raw text format (no links)
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.17.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-