{PDOC00606} {PS00743; BETA_LACTAMASE_B_1} {PS00744; BETA_LACTAMASE_B_2} {BEGIN} ************************************** * Beta-lactamases class B signatures * ************************************** 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 [2]. Class-B enzymes are zinc containing proteins whilst class -A, C and D enzymes are serine hydrolases. Class-B beta-lactamases have been described in several Gram-negative bacterial species; they seem to share the characteristic of being able to hydrolyze carbapenem compounds which are new beta-lactam antibiotics of great therapeutic potential. There are a number of conserved regions in the sequence of known class-B beta- lactamases [3]. Most of them are centered on residues known [4] to be involved in binding the zinc ion essential for the enzyme's catalytic activity. We designed two signature patterns for this class of enzyme. The first contains three residues involved in binding zinc ions. The second pattern contains a cysteine which is also a zinc ligand. -Consensus pattern: [LI]-x-[STN]-[HN]-x-H-[GSTAD]-D-x(2)-G-[GP]-x(7,8)-[GS] [H/N, H and D are zinc ligands] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: P-x(3)-[LIVM](2)-x-G-x-C-[LIVMF](2)-K [C is a zinc ligand] -Sequences known to belong to this class detected by the pattern: ALL, except for L1 from Xanthomonas maltophilia. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2003 / Patterns and text 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] Bush K. "Characterization of beta-lactamases." Antimicrob. Agents Chemother. 33:259-263(1989). PubMed=2658779 [ 3] Osano E., Arakawa Y., Wacharotayankun R., Ohta M., Horii T., Ito H., Yoshimura F., Kato N. "Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance." Antimicrob. Agents Chemother. 38:71-78(1994). PubMed=8141584 [ 4] Concha N.O., Rasmussen B.A., Bush K., Herzberg O. "Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis." Structure 4:823-836(1996). PubMed=8805566 -------------------------------------------------------------------------------- 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}