Inhibition of Serine Proteases by Arylboronic Acids
- 1 February 1971
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 68 (2), 478-480
- https://doi.org/10.1073/pnas.68.2.478
Abstract
Arylboronic acids were found to be strong competitive inhibitors of subtilisin and chymotrypsin. The binding constants are strongly pH dependent and give a Hammett-type plot with a slope of -0.885. The pH dependence, the Hammett plot, and nmr model-system studies indicate that inhibition is due to electron-pair donation by the active site histidine to the bound inhibitor.Keywords
This publication has 6 references indexed in Scilit:
- Binding of competitive inhibitors to δ-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurementsBiochemistry, 1970
- n‐Alkylboronic acids as bifunctional reversible inhibitors of α‐chymotrypsinFEBS Letters, 1970
- Esteratic Reactions Catalyzed by SubtilisinsJournal of Biological Chemistry, 1967
- The Reactivity of Thiol-subtilisin, an Enzyme Containing a Synthetic Functional Group*Biochemistry, 1967
- Spectral studies of the interaction of alpha-chymotrypsin and trypsin with proflavine.Proceedings of the National Academy of Sciences, 1965
- A spectrophotometric determination of trypsin and chymotrypsinBiochimica et Biophysica Acta, 1955