Reference: Myers JS and Jakoby WB (1975) Glycerol as an agent eliciting small conformational changes in alcohol dehydrogenase. J Biol Chem 250(10):3785-9

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Abstract


Yeast alcohol dehydrogenase is an example of a protein in which the K-m for substrate is substantially decreased by the presence of glycerol. The polyol has the effect at pH 8.0 or above of decreasing K-m and K-s for substrate and of altering both the protein's intrinsic fluorescence and ultraviolet absorption difference spectrum. The relationship between each of thse parameters and glycerol concentration displays a transition at a glycerol concentration of 20%. Circular dichroism values for the enzyme are not affected by glycerol over a large range of concentration and temperature. Treatment of the enzyme with glutaraldehyde results in the formation of cross-linked tetramers, the K-m of which are not altered by the presence of the solvent. The data are interpreted as reflecting a change in the conformation of the protein induced by glycerol.

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Myers JS, Jakoby WB
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