Inhibition Studies on Liver Alcohol Dehydrogenase
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چکیده
منابع مشابه
Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies.
The Drosophila melanogaster alleloenzymes AdhS and AdhF have been studied with respect to product inhibition by using the two substrate couples propan-2-ol/acetone and ethanol/acetaldehyde together with the coenzyme couple NAD+/NADH. With both substrate couples the reaction was consistent with an ordered Bi Bi mechanism. The substrates added to the enzyme in a compulsory order, with coenzyme as...
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The study of inorganic tin (SnCl(2), SnCl(4)) and methyltin compounds (MeSnCl(3), Me(2)SnCI(2), Me(3)SnCl) effects on the enzymatic activity of alcohol dehydrogenase (ADH) in the reaction of ethanol oxidation has been carried out. The experimental results of the study show that inorganic tin and methyltin substances induce slight inhibition of the catalytic activity of horse liver alcohol dehyd...
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Reductive methylation of lysine residues activates liver alcohol dehydrogenase in the oxidation of primary alcohols, but decreases the activity of the enzyme towards secondary alcohols. The modification also desensitizes the dehydrogenase to substrate inhibition at high alcohol concentrations. Steady-state kinetic studies of methylated liver alcohol dehydrogenase over a wide range of alcohol co...
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Alcohol dehydrogenase (ADH) is an enzyme in the human body that processes the alcohol concentration in the blood. Alcohol dehydrogenase is a dimer which means it’s a molecule that consists of two parts which are called monomers. There are seven different dehydrogenases. ADH can be found in many organisms and it facilitates the oxidisation of alcohols to aldehydes or ketones and at the same time...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1968
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1968.tb00247.x