CATH Classification

Domain Context

CATH Clusters

Superfamily DD-peptidase/beta-lactamase superfamily
Functional Family D-alanyl-D-alanine serine-type carboxypeptidase

Enzyme Information

3.4.16.4
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P0AEB2
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
-!- A group of bacterial enzymes, membrane-bound. -!- Inhibited by beta-lactam antibiotics, which acylate the active site serine in the enzyme. -!- Distinct from EC 3.4.17.14. -!- Belongs to peptidase families S11, S12 and S13.
3.5.2.6
Beta-lactamase.
based on mapping to UniProt P0AEB2
A beta-lactam + H(2)O = a substituted beta-amino acid.
-!- Zinc is only requires in class-B enzymes. -!- A group of enzymes of varying specificity hydrolyzing beta-lactams; some act more rapidly on penicillins, some more rapidly on cephalosporins. -!- Formerly EC 3.5.2.8.

UniProtKB Entries (1)

P0AEB2
DACA_ECOLI
Escherichia coli K-12
D-alanyl-D-alanine carboxypeptidase DacA

PDB Structure

PDB 1NZO
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex.
Nicholas, R.A., Krings, S., Tomberg, J., Nicola, G., Davies, C.
J.Biol.Chem.