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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-gamma-D-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-gamma-D-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

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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.-.-.-