Potent and selective inactivation of proteinases with N-peptidyl-O-acylhydroxylamines.
The reaction of seven N-peptidyl-O-acyl hydroxylamines with serine proteinases exhibiting different substrate specificity has been investigated. Depending on the structure of the peptidyl residue of the inhibitors, rapid and complete irreversible inactivation of the enzymes may be achieved. Enzyme-catalyzed turnover of inhibitor to products was detected during reaction of proline-specific endopeptidase with N-Boc-Ala-Pro-O-(4-nitrobenzoyl)hydroxylamine.
Demuth
H U
HU
Department of Biotechnology, Martin-Luther-University of Halle, G.D.R.
Schönlein
C
C
Barth
A
A
D010450:Endopeptidases; D006898:Hydroxylamines / Q000138:chemical synthesis / Q000494:pharmacology*; D066298:In Vitro Techniques; D007700:Kinetics; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors; D013329:Structure-Activity Relationship; D013381:Subtilisins / Q000037:antagonists & inhibitors
D006898:Hydroxylamines; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins; C022728:thermitase; D010196:Pancreatic Elastase