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Updated: Aug 11, 2026

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
Published on: October 2, 2012
[Effect of alcohols on the activity of bacterial agmatinase]
Abstract:
Aliphatic alcohols inhibit the activity of bacterial agmatinase (E. C. 3.5.3.11). A correlation is demonstrated between the inhibition constant and the length of alcohol carbohydrate radical, and the presence of polar groups has decreased the inhibitory effect. The importance of hydrophobic interactions in the formation of agmatinase-substrate and agmatinase-inhibitor complexes is suggested. The increment of free binding energy within the homologous alcohol row is practically constant (0.5-0.7 kcal/mole). Comparison of deltaF amines and their respective alcohols makes possible to evaluate the contribution of electrostatic interaction in the formation of the enzyme-inhibitor complex. A correlation is observed between solubility of alcohols and their inhibitory effect.
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