Active Site

Beta-lactamase, class-D active site (IPR002137)

Short name: Beta-lactam_class-D_AS

Description

Beta-lactamases (EC:3.5.2.6) [PMID: 6109327, PMID: 2082152] 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 [PMID: 2658779]. 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 [PMID: 3128280] 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.

GO terms

Biological Process

GO:0017001 antibiotic catabolic process

Molecular Function

GO:0008800 beta-lactamase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns