Use of electrospray mass spectrometry to directly observe an acyl enzyme intermediate in beta-lactamase catalysis.
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.
Aplin
R T
RT
Dysons Perrins Laboratory, Oxford, UK.
Baldwin
J E
JE
Schofield
C J
CJ
Waley
S G
SG
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*
D000900:Anti-Bacterial Agents; D001618:beta-Lactamases; D002228:Carbenicillin