Structure–reactivity relationships in the inactivation of elastase by β-sultams
PS Hinchliffe, JM Wood, AM Davis, RP Austin…
文献索引：Hinchliffe, Paul S.; Wood, J. Matthew; Davis, Andrew M.; Austin, Rupert P.; Beckett, R. Paul; Page, Michael I. Organic and Biomolecular Chemistry, 2003 , vol. 1, # 1 p. 67 - 80
N-Acyl-β-sultams are time dependent irreversible active site directed inhibitors of elastase. The rate of inactivation is first order with respect to β-sultam concentration and the second order rate constants show a similar dependence on pH to that for the hydrolysis of a peptide substrate. Inactivation is due to the formation of a stable l∶ l enzyme inhibitor complex as a result of the active site serine being sulfonylated by the β-sultam. Ring opening of the β- ...
