KEGG   ENZYME: 3.4.17.8
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
Reaction(IUBMB)
Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-6-carboxy-L-lysyl-D-alanyl!D-alanine [RN:R08850]
Reaction(KEGG)
R08850;
(other) R04611
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-gamma-D-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 243:3193-201 (1968)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.17.8
IUBMB Enzyme Nomenclature: 3.4.17.8
ExPASy - ENZYME nomenclature database: 3.4.17.8
BRENDA, the Enzyme Database: 3.4.17.8
CAS: 9077-67-2

  All links  
Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (4)   
   KEGG REACTION (2)   
   KEGG RCLASS (2)   
Protein sequence (18)   
   UniProt (17)   
   PDBSTR (1)   
DNA sequence (50)   
   GenBank (25)   
   EMBL (25)   
3D Structure (1)   
   PDB (1)   
All databases (79)   

Download RDF
DBGET integrated database retrieval system