Inhibition of Chymotrypsin and Pancreatic Elastase by4H-3, 1-Benzoxazin-4-Ones
- 1 January 1991
- journal article
- research article
- Published by Taylor & Francis in Journal of Enzyme Inhibition
- Vol. 4 (3), 227-232
- https://doi.org/10.3109/14756369109035846
Abstract
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.Keywords
This publication has 15 references indexed in Scilit:
- Crystal structures of the complex of porcine pancreatic elastase with two valine-derived benzoxazinone inhibitorsJournal of Molecular Biology, 1987
- Mechanism for slow-binding inhibition of human leukocyte elastase by valine-derived benzoxazinonesBiochemistry, 1987
- Design of alternate substrate inhibitors of serine proteases. Synergistic use of alkyl substitution to impede enzyme-catalyzed deacylationJournal of Medicinal Chemistry, 1987
- Inhibition of serine proteases by benzoxazinones: effects of electron withdrawal and 5-substitutionBiochemical and Biophysical Research Communications, 1986
- Mechanism of inactivation of chymotrypsin by 3-benzyl-6-chloro-2-pyroneBiochemistry, 1984
- Suicide inactivation of chymotrypsin by benzoxazinonesBiochemistry, 1984
- New class of serine protease inactivators based on isatoic anhydrideJournal of the American Chemical Society, 1982
- [7] ElastaseMethods in Enzymology, 1970
- [5] Chymotrypsinogens—chymotrypsinsPublished by Elsevier ,1970
- The Anatomy of an Enzymatic Catalysis. α-ChymotrypsinJournal of the American Chemical Society, 1964