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Yasuhito Yamamoto, Hideo Kise, Concentration- and Structure-Dependent Effects of Amides on Protease Activity in Organic Solvents, Bulletin of the Chemical Society of Japan, Volume 67, Issue 5, May 1994, Pages 1367–1370, https://doi.org/10.1246/bcsj.67.1367
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Abstract
The catalytic activity of α-chymotrypsin (CT) in the transesterification of N-acetyl-l-tyrosine methyl ester to its ethyl ester in aqueous-organic media was markedly enhanced by replacing a part of water with formamide. The activity of CT was strongly dependent on the formamide/water ratio, and excess formamide retarded the activity. Addition of formamide to reaction mixtures at constant water contents exhibited similar activation–deactivation profiles for CT. A kinetic study revealed that the rate acceleration is due to an increase in kcat rather than a change in Km. At a given concentration of amides (0.5 M, M = mol dm−3), propionamide and DMF were much less effective than formamide for activation of CT. The results suggest that formamide interacts with CT in a different way from water.