title: Succinimide and saccharin-based enzyme-activated inhibitors of serine proteases.
abstract: The inhibition of human leukocyte elastase (HLE), and other serine proteases, by succinimide and saccharin-based compounds is reviewed. The succinimide compounds are unique in that the inactivating species is generated within the enzyme active site via a molecular rearrangement. The related saccharin derivatives also inactivate serine proteases by an enzyme-activated mechanism. Those factors effecting the potency, selectivity and stability of these important classes of inhibitor are discussed.
authors.affiliation: Department of Chemistry, University of Canterbury, Christchurch, New Zealand.
authors.forename: D C
authors.initials: DC
authors.lastname: Martyn
authors.forename: M J
authors.initials: MJ
authors.lastname: Moore
authors.forename: A D
authors.initials: AD
authors.lastname: Abell
mesh_terms: D001665:Binding Sites; D006801:Humans; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors*; D012439:Saccharin / Q000494:pharmacology*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013388:Succinimides / Q000494:pharmacology*
chemical_list: D015842:Serine Proteinase Inhibitors; D013388:Succinimides; C032620:succinimide; D019272:Leukocyte Elastase; D012439:Saccharin