Inhibition of chymotrypsin and pancreatic elastase by 4H-3,1-benzoxazin-4-ones.
Eight 3,1-Benzoxazin-4-ones have been used to inactivate chymotrypsin and pancreatic elastase. Whereas 6,7-dimethoxy substitution only slightly decreased the acylation rate constant, the deacylation reaction was nearly unaffected. Bulky alkoxy groups in position 2 of the heterocyclic moiety were shown to increase enormously the acylation rate of chymotrypsin, but not that of elastase.
Neumann
U
U
Institute of Pharmacology and Toxicology, Medical Academy Erfurt, G.D.R.
Stürzebecher
J
J
Leistner
S
S
Vieweg
H
H
D000215:Acylation; D001667:Binding, Competitive; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D007700:Kinetics; D010078:Oxazines / Q000494:pharmacology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D013329:Structure-Activity Relationship
D010078:Oxazines; D002918:Chymotrypsin; D010196:Pancreatic Elastase