Glycerol as an agent eliciting small conformational changes in alcohol dehydrogenase

Autor:	W B Jakoby, J S Myers
Rok vydání:	1975
Předmět:	chemistry.chemical_classification Circular dichroism biology Stereochemistry Substrate (chemistry) Cell Biology Biochemistry Solvent chemistry.chemical_compound Enzyme chemistry Polyol Glycerol biology.protein Biophysics Glutaraldehyde Molecular Biology Alcohol dehydrogenase
Zdroj:	Journal of Biological Chemistry. 250:3785-3789
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(19)41467-1
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::6af0aa9a732f5d03f09db12092ce3bee https://doi.org/10.1016/s0021-9258(19)41467-1 Zobrazit plný text záznamu