PMID- 8471035 OWN - NLM STAT- MEDLINE DA - 19930512 DCOM- 19930512 LR - 20091118 IS - 0264-6021 (Print) IS - 0264-6021 (Linking) VI - 291 ( Pt 1) DP - 1993 Apr 1 TI - An overview of the kinetic parameters of class B beta-lactamases. PG - 151-5 AB - The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila beta-lactamase exhibited a unique specificity profile and could be considered as a rather specific 'carbapenemase'. No relationships were found between sequence similarities and catalytic properties. The problem of the repartition of class B beta-lactamases into sub-classes is discussed. Improved purification methods were devised for the P. maltophilia and A. hydrophila beta-lactamases including, for the latter enzyme, a very efficient affinity chromatography step on a Zn(2+)-chelate column. AD - Universita degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Italy. FAU - Felici, A AU - Felici A FAU - Amicosante, G AU - Amicosante G FAU - Oratore, A AU - Oratore A FAU - Strom, R AU - Strom R FAU - Ledent, P AU - Ledent P FAU - Joris, B AU - Joris B FAU - Fanuel, L AU - Fanuel L FAU - Frere, J M AU - Frere JM LA - eng PT - Comparative Study PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - ENGLAND TA - Biochem J JT - The Biochemical journal JID - 2984726R RN - EC 3.5.2.6 (beta-Lactamases) SB - IM MH - Aeromonas hydrophila/enzymology MH - Bacillus cereus/enzymology MH - Catalysis MH - Electrophoresis, Polyacrylamide Gel MH - Isoelectric Point MH - Kinetics MH - Molecular Weight MH - Pseudomonas/enzymology MH - beta-Lactamases/chemistry/isolation & purification/*metabolism PMC - PMC1132494 OID - NLM: PMC1132494 EDAT- 1993/04/01 MHDA- 1993/04/01 00:01 CRDT- 1993/04/01 00:00 PST - ppublish SO - Biochem J. 1993 Apr 1;291 ( Pt 1):151-5.