ALCOHOL DEHYDROGENASE: Structure and Function
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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 کاملThe physiological role of liver alcohol dehydrogenase.
1. Yeast alcohol dehydrogenase was used to determine ethanol in the portal and hepatic veins and in the contents of the alimentary canal of rats given a diet free from ethanol. Measurable amounts of a substance behaving like ethanol were found. Its rate of interaction with yeast alcohol dehydrogenase and its volatility indicate that the substance measured was in fact ethanol. 2. The mean alcoho...
متن کاملNormal testicular structure and reproductive function in deermice lacking retinol and alcohol dehydrogenase activity.
It was found that a strain of deermice (Peromyscus maniculatus), which genetically lacks liver alcohol dehydrogenase activity also displays no such activity in the testis and is devoid of the enzyme activity that converts retinol to retinal, both in liver and in the testis; nevertheless, these animals exhibit normal reproduction and testicular histology. Therefore, one must reconsider the theor...
متن کاملTime-dependent XAS studies of trapped enzyme-substrate complexes of alcohol dehydrogenase from Thermoanaerobacter brockii.
The understanding of structure-function relationships in proteins has been significantly advanced with the advent of the biotechnological revolution. A goal yet to be realized for many metalloenzyme systems is to characterize the dynamic changes in structure that bridge the static endpoints provided by crystallography. We present here a series of edge and EXAFS spectra of the metalloenzyme alco...
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