CATH Classification

Domain Context

CATH Clusters

Superfamily Penicillin-binding protein 2a (Domain 2)
Functional Family

Enzyme Information

3.4.16.4
Serine-type D-Ala-D-Ala carboxypeptidase.
based on mapping to UniProt P08149
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.

UniProtKB Entries (1)

P08149
PBP2_NEIGO
Neisseria gonorrhoeae
Probable peptidoglycan D,D-transpeptidase PenA

PDB Structure

PDB 3EQU
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal Structures of Penicillin-binding Protein 2 from Penicillin-susceptible and -resistant Strains of Neisseria gonorrhoeae Reveal an Unexpectedly Subtle Mechanism for Antibiotic Resistance.
Powell, A.J., Tomberg, J., Deacon, A.M., Nicholas, R.A., Davies, C.
J.Biol.Chem.