for E, values, calculate AG" for oxidation of malate by malate dehydrogenase.
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The reaction is
NAD+ + Malate ---> NADH + oxaloacetate + H+
Step by step
Solved in 2 steps
- , which indicates AG for each glycolytic reac- tion under intracellular conditions. Assume that glyceraldehyde-3- phosphate dehydrogenase was inhibited with iodoacetic acid. Which glycolytic intermediate would you expect to accumulate most rapidly, and why?Referring to for E′0 values, calculate ΔG°′ for oxidation of malate by malate dehydrogenase.Outline the mechanism of the conversion of a-ketoglutarate to succinylCoA catalyzed by α-ketoglutarate dehydrogenase complex. Include all products, coenzymes, and reactions in your discussion.
- The reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this says about the occurrence of the reaction catalyzed by malate dehydrogenase in cells explain how the reaction catalyzed by citrate synthase (−31.5 kJ⋅mol−1) influences that activity of malate dehydrogenase. In addition, explain how the activity of citrate synthase functions as a regulatory point for the citric acid cycleWhat is alpha keto glutarate dehydrogenase complex?. explain very briefly.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?
- Why Alpha-Ketoglutarate dehydrogenase (a-KGDH) called deficiency? What are the probable causes? Explain.The mechanism for the conversion from alpha kytoglutarate into succinyl CoA by alpha-ketoglutare dehydrogenase is analogous to the pyruvate dehydrogenase mechanism. Draw and show the major intermediates and arrow pushing for the enzyme-catalyze process for the conversion of alpha-ketoglutarate to succinyl CoA. Note: the carbanion of thiamine pyrophosphate nucleophillically attacks C-2 of the alpha-ketoglutarate, i.e., the carbonyl carbon of that substrate.Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
- Alpha-ketoglutarate dehydrogenase exhibits feedback inhibition byIndicate what will happen (increase, decrease or no effect) to the activity of enzyme or rate of the metabolic pathway given the following conditions: 1. epinephrine to the activity of glycogen synthase 2. high [2-carboxyarabinitol-1-phosphate] to the carboxylase activity of RuBisCOWhen the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.