Glycerol as an agent eliciting small conformational changes in alcohol dehydrogenase.
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.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D001665:Binding Sites; D002850:Chromatography, Gel; D002942:Circular Dichroism; D005990:Glycerol / Q000494:pharmacology; D007700:Kinetics; D009243:NAD / Q000031:analogs & derivatives; D011485:Protein Binding; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D013997:Time Factors
D009243:NAD; D000429:Alcohol Oxidoreductases; D005990:Glycerol