Acrolein, an irreversible active-site-directed inhibitor of deoxyribose 5-phosphate aldolase?
The enzyme deoxyribose 5-phosphate aldolase was irreversibly inactivated by the substrate analogue acrolein with a pseudo-first-order rate constant of 0.324 min-1 and a Ki (apparent) of 2.7 x 10(-4) m. No inactivation was observed after prolonged incubation with the epoxide analogues glycidol phosphate and glycidaldehyde. It is suggested that the acrolein is first activated by forming a Schiff base with the enzyme active-site lysine residue and it is the activated inhibitor that reacts with a suitable-active-site nucleophile.
D000171:Acrolein / Q000494:pharmacology*; D000446:Aldehyde-Lyases / Q000037:antagonists & inhibitors*; D000447:Aldehydes / Q000494:pharmacology*; D001665:Binding Sites; D004852:Epoxy Compounds / Q000494:pharmacology; D007700:Kinetics; D012267:Ribosemonophosphates; D012486:Salmonella typhimurium / Q000201:enzymology
D000447:Aldehydes; D004852:Epoxy Compounds; D012267:Ribosemonophosphates; D000171:Acrolein; D000446:Aldehyde-Lyases