Equilibria and Substrate Specificity Studies with Alcohol Dehydrogenases
نویسندگان
چکیده
منابع مشابه
Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.
A three-dimensional model of yeast alcohol dehydrogenase, based on the homologous horse liver enzyme, was used to compare the substrate binding pockets of the three isozymes (I, II, and III) from Saccharomyces cerevisiae and the enzyme from Schizosaccharomyces pombe. Isozyme I and the S. pombe enzyme have methionine at position 294 (numbered as in the liver enzyme, corresponding to 270 in yeast...
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Nicotine adenine dinucleotide-linked primary alcohol dehydrogenase and a newly discovered secondary alcohol dehydrogenase coexist in most strains of methanol-grown yeasts. Alcohol dehydrogenases from methanol-grown yeasts oxidize (--)-2-butanol preferentially over its (+) enantiomorph. This is substantially different from alcohol dehydrogenases from bakers' yeast and horse liver.
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Hyphomicrobium strain WC, Pseudomonas strain TP-1, and Pseudomonas strain W1 are capable of growth on methanol as the sole source of carbon and energy. Methanol-grown cells of each organism contain a primary alcohol dehydrogenase that has been purified to homogeneity. Each enzyme has a molecular weight of 120,000 and shows an in vitro requirement for phenazine methosulfate and ammonium ions for...
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In Aspergillus nidulans three alcohol dehydrogenases (ADHs) have been described. ADHI is induced by ethanol and is the physiological enzyme of ethanol utilization, ADHII has not been attributed a function but is repressed by ethanol. The ALCR regulatory protein acts positively to induce ADHI, and negatively in its control of ADHII. ADHIII is specifically induced by anaerobic stress. We have cha...
متن کاملAlcohol dehydrogenases and aldehyde dehydrogenases.
T h e structure, function and evolution of alcohol dehydrogenases and aldehyde dehydrogenases have been studied for several years. Recent progress o n these aspects has been considerable and allows extensive conclusions to be drawn about the relationships and properties of these enzymes. Further aspects have also become available for study, such as the regulation of enzyme expression and the an...
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ژورنال
عنوان ژورنال: Bulletin of the Chemical Society of Japan
سال: 1976
ISSN: 0009-2673,1348-0634
DOI: 10.1246/bcsj.49.214