title: Extended-spectrum beta-lactamases: structure and kinetic mechanism.
abstract: Recent years have seen an explosion in the numbers of extented spectrum class A beta-lactamases (ESBLs). The steady-state kinetic parameters for hydrolysis of beta-lactams by ESBLs is discussed in the light of what is known about the structure of these mutant enzymes.
authors.affiliation: Basilea Pharmaceutica Ltd, Basel, Switzerland. malcolm.page@basilea.com
authors.forename: M G P
authors.initials: MG
authors.lastname: Page
mesh_terms: D006090:Gram-Negative Bacteria / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D047090:beta-Lactams / Q000737:chemistry / Q000145:classification / Q000378:metabolism*
chemical_list: D065093:beta-Lactamase Inhibitors; D047090:beta-Lactams; D001618:beta-Lactamases