What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?
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What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol
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- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.Alcohol dehydrogenase catalyzes the oxidation of an alcohol to the next highest state of oxidation, an aldehyde. How does this partially explain the toxicity of methanol?
- What is the enzyme classification of the catalyst used in the conversionof oxalosuccinate to alpha-ketoglutarate?Refer to Figure, which indicates ∆G for each glycolytic reaction under intracellular conditions. Assume that glyceraldehyde-3-phosphate dehydrogenase was inhibited with iodoacetate, which reacts with its active site cysteine sulfhydryl group. Which glycolytic intermediate would you expect to accumulate most rapidly, and why?Intestinal microbes produce butyrate, which helps regulate the immune system. How many rounds of β oxidation of palmitate are required to produce butyrate?
- The metabolism of alcohol pathway is showed in the figure characterized by biotransformation of: (Figure : Ethanol Metabolism Pathway - ADH : Alcohol dehydrogenases, ALDH: Aldehyde dehydrogenase ) (a) reaction phase I with two oxidations (b) reaction phase II with oxidation and sulfonation (c) reaction phase II with two hydrolysations (d) reaction phase II with two oxidations (e) reaction phase I with hydrolysis and oxidationIn some brain cancer cells, a mutated form of isocitrate dehydrogenase, instead of catalyzing the oxidation of the secondary alcohol of isocitrate, catalyzes the reduction of a-ketoglutarate. Draw the product of the reaction.The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.
