| Entry |
|
|---|
| 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-D-gamma-glutamyl-6-carboxy-L-lysyl-D-
alanyl!D-alanine [RN:R08850] |
|---|
| Reaction(KEGG) |
R08850;
(other) R04611
 |
|---|
| Inhibitor |
Penicillin [CPD:C00395];
Cephalosporin [CPD:C00875] |
|---|
| Effector |
Divalent metal [CPD:C02148] |
|---|
| 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. |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:4871206]
Izaki K, Strominger JL.
Biosynthesis of the peptidoglycan of bacterial cell walls. XIV.
Purification and properties of two D-alanine carboxypeptidases from
Escherichia coli.
J. Biol. Chem. 243 (1968) 3193-201.
Escherichia coli [GN:eco] |
|---|
| 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 |
|---|
