| Type: | Active_site | Name: | Beta-lactamase, class-D active site |
| Description: | Beta-lactamases () [, ] are enzymes which catalyze the hydrolysis of an amide bond in the beta-lactam ring of antibiotics belonging to the penicillin/cephalosporin family. Four kinds of beta-lactamase have been identified []. Class-B enzymes are zinc containing proteins whilst class -A, C and D enzymes are serine hydrolases. The three classes of serine beta-lactamases are evolutionary related and belong to a superfamily [] that also includes DD-peptidases and a variety of other penicillin-binding proteins (PBP's). All these proteins contain a Ser-x-x-Lys motif, where the serine is the active site residue. Although clearly homologous, the sequences of the three classes of serine beta-lactamases exhibit a large degree of variability and only a small number of residues are conserved in addition to the catalytic serine.This active site signature detects all class D Beta-lactamases. | Short Name: | Beta-lactam_class-D_AS |
