{PDOC00134} {PS00146; BETA_LACTAMASE_A} {PS00336; BETA_LACTAMASE_C} {PS00337; BETA_LACTAMASE_D} {BEGIN} ****************************************************** * Beta-lactamases classes -A, -C, and -D active site * ****************************************************** Beta-lactamases (EC 3.5.2.6) [1,2] 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 [3]. 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 [4] 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. Since a pattern detecting all serine beta-lactamases would also pick up many unrelated sequences, we decided to provide specific patterns, centered on the active site serine, for each of the three classes. -Consensus pattern: [FY]-x-[LIVMFY]-{E}-S-[TV]-x-K-x(3)-{T}-[AGLM]-{D}-{KA}- [LC] [S is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL class-A beta-lactamases. -Other sequence(s) detected in Swiss-Prot: 7. -Consensus pattern: [FY]-E-[LIVM]-G-S-[LIVMG]-[SA]-K [The first S is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL class-C beta-lactamases. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [PA]-x-S-[ST]-F-K-[LIV]-[PALV]-x-[STA]-[LI] [S is the active site residue] -Sequences known to belong to this class detected by the pattern: ALL class-D beta-lactamases. -Other sequence(s) detected in Swiss-Prot: NONE. -Expert(s) to contact by email: Brannigan J.; jab5@vaxa.york.ac.uk -Last update: April 2006 / Pattern revised. [ 1] Ambler R.P. "The structure of beta-lactamases." Philos. Trans. R. Soc. Lond., B, Biol. Sci. 289:321-331(1980). PubMed=6109327 [ 2] Pastor N., Pinero D., Valdes A.M., Soberon X. "Molecular evolution of class A beta-lactamases: phylogeny and patterns of sequence conservation." Mol. Microbiol. 4:1957-1965(1990). PubMed=2082152 [ 3] Bush K. "Characterization of beta-lactamases." Antimicrob. Agents Chemother. 33:259-263(1989). PubMed=2658779 [ 4] Joris B., Ghuysen J.-M., Dive G., Renard A., Dideberg O., Charlier P., Frere J.M., Kelly J.A., Boyington J.C., Moews P.C. "The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family." Biochem. J. 250:313-324(1988). PubMed=3128280 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}