title: Use of electrospray mass spectrometry to directly observe an acyl enzyme intermediate in beta-lactamase catalysis.
abstract: Electrospray mass spectrometry was used to directly observe intact acyl enzyme complexes formed between a class C beta-lactamase (from Enterobacter cloacae P99) and four poor substrates/inhibitors. In each case the molecular weight difference between the unreacted and the reacted beta-lactamase was consistent with the formation of an acyl enzyme.
authors: Dysons Perrins Laboratory, Oxford, UK.
authors: R T
authors: RT
authors: Aplin
authors: J E
authors: JE
authors: Baldwin
authors: C J
authors: CJ
authors: Schofield
authors: S G
authors: SG
authors: Waley
mesh_terms: D000215:Acylation; D000900:Anti-Bacterial Agents / Q000378:metabolism; D002228:Carbenicillin / Q000737:chemistry; D004754:Enterobacter / Q000201:enzymology; D013058:Mass Spectrometry / Q000379:methods*; D008970:Molecular Weight; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D001618:beta-Lactamases; D002228:Carbenicillin