Conformational changes and catalysis by alcohol dehydrogenase
نویسندگان
چکیده
منابع مشابه
Yeast Alcohol Dehydrogenase Structure and Catalysis
Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose. ADH1 is a homotetramer of subunits with 347 amino acid residues. A structure for ADH1 was determined by X-ray crystallography at 2.4 Å resolution. The asymmetric unit contains four different subunits, arranged as similar dimers named...
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During catalysis by liver alcohol dehydrogenase (ADH), a water bound to the catalytic zinc is replaced by the oxygen of the substrates. The mechanism might involve a pentacoordinated zinc or a double-displacement reaction with participation by a nearby glutamate residue, as suggested by studies of human ADH3, yeast ADH1, and some other tetrameric ADHs. Zinc coordination and participation of wat...
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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 co...
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The effect of pH on steady state kinetic parameters for the yeast alcohol dehydrogenase-catalyzed reduction of aldehydes and oxidation of alcohols has been studied. The oxidation of p-CH3 benzyl alcohol-1,1-h2 and -1,1-d2 by NAD+ was found to be characterized by large deuterium isotope effects (kH/kD = 4.1 plus or minus 0.1) between pH 7.5 and 9.5, indicating a rate-limiting hydride trahsfer st...
متن کاملAcid-Base Catalysis in the Yeast Alcohol Dehydrogenase Reaction*
The effect of pH on steady state kinetic parameters for the yeast alcohol dehydrogenase-catalyzed reduction of aldehydes and oxidation of alcohols has been studied. The oxidation of p-CH3 benzyl alcohol-l, l-h2 and -l,l-dz by NAD+ was found to be characterized by large deuterium isotope effects (&J&n = 4.1 f 0.1) between pH 7.5 and 9.5, indicating a rate-limiting hydride transfer step in this p...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2010
ISSN: 0003-9861
DOI: 10.1016/j.abb.2009.07.001