Benzoate catalysis in the hydrolysis of endo -5-[4′(5′)imidazolyl]-bicyclo[2.2.1]hept- endo - 2-yl trans -cinnamate: Implications for the charge-transfer mechanism of catalysis by serine proteases
- 1 June 1980
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 77 (6), 3095-3097
- https://doi.org/10.1073/pnas.77.6.3095
Abstract
The acceleration, by a factor of 2500, of the hydrolysis of endo-5-[4''(5'')imidazolyl]bicyclo[2.2.1]hept-endo-2-yl trans-cinnamate by 0.5 M sodium benzoate in 42 mol % dioxane in water can be explained without resort to operation of a charge-relay mechanism similar to that often postulated to account for the enzymatic activity of serine proteases. The degree of ionization of 4-methylimidazole and of sodium benzoate in 42 mol % dioxane in water at 60.degree. C were measured by NMR spectroscopy.This publication has 8 references indexed in Scilit:
- Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteasesJournal of the American Chemical Society, 1978
- Energetics of enzyme catalysis.Proceedings of the National Academy of Sciences, 1978
- Model for “charge-relay”: Acceleration by carboxylate anion in intramolecular general base-catalyzed ester hydrolysis by the imidazolyl groupProceedings of the National Academy of Sciences, 1977
- Intramolecular general base-catalyzed ester hydrolyses by the imidazolyl group.Proceedings of the National Academy of Sciences, 1977
- Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transferBiochemistry, 1976
- Applications of natural-abundance nitrogen-15 nuclear magnetic resonance to large biochemically important molecules.Proceedings of the National Academy of Sciences, 1975
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969