Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis
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چکیده
منابع مشابه
Biochemical characterization of recombinant benzyl alcohol dehydrogenase from Rhodococcus ruber UKMP-5M
Benzyl Alcohol Dehydrogenase (BADH) is an important enzyme for hydrocarbon degradation, which can oxidize benzyl alcohols to aldehydes, while being capable of catalyzing a reversible reaction by reducing benzaldehyde. BADH is a member of medium chain alcohol dehydrogenases, in which zinc and NAD are essential for enzyme activity. This paper describes the expression, purification, and characteri...
متن کاملBiochemical characterization of recombinant benzyl alcohol dehydrogenase from Rhodococcus ruber UKMP-5M
Benzyl Alcohol Dehydrogenase (BADH) is an important enzyme for hydrocarbon degradation, which can oxidize benzyl alcohols to aldehydes, while being capable of catalyzing a reversible reaction by reducing benzaldehyde. BADH is a member of medium chain alcohol dehydrogenases, in which zinc and NAD are essential for enzyme activity. This paper describes the expression, purification, and characteri...
متن کاملDrosophila Alcohol Dehydrogenase
Drosophila alcohol dehydrogenasc (alcohol:NADf oxidorcduct.ase, EC 1.1.1.1) has attracted attention in several laboratories (l-3) recently. Genetic variants of this enzyme were found, and consequently it was possible to determine its structural locus on the genetic map. The specific activity of alcohol dehydrogenase varies greatly along the t.ime axis of devcloprnent of this organism, and it oc...
متن کاملInterconversion of Isoenzymes of Drosophila Alcohol Dehydrogenase
Drosophila alcohol dehydrogenase and its subunits were examined for their physical characteristics. The intact enzyme was shown to have a molecular weight of approximately 60,000. The smallest apparent subunit was obtained by dissociating the enzyme with sodium dodecylsulfate and the molecular weight obtained was 7,500. Evidence for three partially dissociated forms was obtained; the subunits o...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1986
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2350481