which statements are false? The standard free energy (AG,') for the reduction of CoQ by FADH2 (consult Table 20.1) is -61.7 kJ/molaCitrate must be isomerized to Isocitrate because the tertiary alcohol group of Citrate is not oxidizable but the secondarybgroup of Isocitrate can be oxidizeda-Ketoglutarate Dehydrogenase is a multi-enzyme complex analogous to Glyceraldehyde 3-Phosphate DehydrogenaseUnder anaerobic conditions skeletal muscle generates lactate from Pyruvate to regenerate NAD+ for further GlycolysisFor the Pyruvate Kinase reaction the correct sequence of events is substrate level phosphorylation - tautomerizationketo form of Pyruvate – enol form of PyruvateeDihydroxyacetone Phosphate is an enantiomer of Glyceraldehyde-3-PhosphateCoQ shuttles electrons from Complex I and Il to Complex IVIf[1-"C] Ribose-5-phosphate is incubated with a mixture of purified transketolase- transaldolase-phosphopentosehisomerase-phosphopentose epimerase and glyceraldehyde-3-phosphate the Erythrose-4-phosphate will be labeled in the1 and 3 positionsiPyruvate Carboxylase activates CO, by ATP through formation of carboxyphosphate as an intermediate

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 12P

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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.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
The Effect of lodoacetic Acid on the Glyceraldehyde-3-P Dehydrogenase Reaction (Integrates with Chapters 4 and 14.) How might iodoacetic acid affect the glyceraldehydes-3-phosphate dehydrogenase reaction in glycolysis? Justify your answer.
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
(b) ☐ The exergonic reactions catalyzed by isocitrate dehydrogenase (ICDH) and α- ketoglutarate dehydroge-nase (aKGDH) are regu- lated by metabolites, in addition to the reaction catalyzed by citrate synthase. The diagram to the right illustrates the activity of ICDH (A,▲) and aKGDH (O,●) in the presence of 1.5 mM ADP (O,A) or 1.5 mM ATP (●,▲). In muscle tissue contraction of sarcomeres initiated by a nerve im- pulse results first in the release of Ca 2+ from the sarcoplasmic reticulum. As indicated by the chang- es in velocity of the two enzymes, what are the flux changes of the TCA cycle in muscle tissue upon release of Ca2+ under the influence of ADP viz. ATP and under the influence of NAD+ viz. NADH on cit- rate synthase? 100 75 Stimulation of activity (% of maximum) ŏ 25 1. -8 -7 -6 log {[Ca2+] (M)}
Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?How detailed is the enzyme structure known below(It's Pyruvate Dehydrogenase )? What insight(s) does this structural detail give you about the enzyme mechanism.
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 cycle
[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. 9 H-C-OH 800- -H CH₂ ° Coo of NAD+ dehydrogen isocitrate ase NADH, H*, Drawing CO2
, 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?
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
Normal carbonic anhydrase has zinc at its active site . Suggest a structural reason why carbonicanhydrase synthesized with Ni²⁺, Fe²⁺, or Mn²⁺ in place of Zn²⁺ gives an enzyme with less catalytic efficiency.

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