
doi: 10.1007/bf02531226
pmid: 4330546
AbstractWe demonstrated two NAD+‐linked alcohol dehydrogenases in cell free extracts ofCandida tropicalis grown onn‐tetradecane. Comparative studies of localization, properties and regulation indicate that these enzymes are involved in two different pathways ofn‐alkane metabolism, one cytoplasmic and the other mitochondrial. Kinetic properties, such as the variation of the Km and Vmax as a function of substrate chain length of the soluble NAD+‐linked alcohol dehydrogenase, might involve hydrophobic interactions between the substrate and the enzyme.
Azides, Cyanides, Hydrocarbons, Halogenated, Iodoacetates, Mercury, Hydroxylamines, Chromatography, DEAE-Cellulose, Alcohol Oxidoreductases, Kinetics, Glucose, Chlorides, Ammonium Sulfate, Alcohols, Enzyme Induction, Alkanes, Chromatography, Gel, Chemical Precipitation, Fatty Alcohols, Chloromercuribenzoates, Candida
Azides, Cyanides, Hydrocarbons, Halogenated, Iodoacetates, Mercury, Hydroxylamines, Chromatography, DEAE-Cellulose, Alcohol Oxidoreductases, Kinetics, Glucose, Chlorides, Ammonium Sulfate, Alcohols, Enzyme Induction, Alkanes, Chromatography, Gel, Chemical Precipitation, Fatty Alcohols, Chloromercuribenzoates, Candida
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