KEGG   ENZYME: 3.4.17.8Help
Entry
EC 3.4.17.8                 Enzyme                                 

Name
muramoylpentapeptide carboxypeptidase;
D-alanine carboxypeptidase I;
DD-carboxypeptidase;
D-alanine carboxypeptidase;
D-alanyl-D-alanine carboxypeptidase;
D-alanine-D-alanine-carboxypeptidase;
carboxypeptidase D-alanyl-D-alanine;
carboxypeptidase I;
UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase;
D-alanyl-D-alanine peptidase;
DD-peptidase;
penicillin binding protein 5;
PBP5;
PdcA;
VanY
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl!D-alanine [RN:R08850]
Reaction(KEGG)
R08850;
(other) R04611
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Comment
A bacterial enzyme that requires a divalent cation for activity. 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.
History
EC 3.4.17.8 created 1972 as EC 3.4.12.6, transferred 1978 to EC 3.4.17.8
Reference
1  [PMID:4871206]
  Authors
Izaki K, Strominger JL.
  Title
Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli.
  Journal
J. Biol. Chem. 243 (1968) 3193-201.
  Organism
Escherichia coli
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9077-67-2

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