For the Oxaloacetate -> Malate reaction, assume the normal ratio of NAD/NADH, what is the maximum ratio of Malate/Oxaloacetate that will allow reaction progress?
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For the Oxaloacetate -> Malate reaction, assume the normal ratio of NAD/NADH, what is the
maximum ratio of Malate/Oxaloacetate that will allow reaction progress?
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- Give a full arrow pushing mechanism of the spontaneous redox reaction between NAD+/NADH and oxaloacetate/malate. Please include diagram drawing of the mechanism! (Thank You!)What is the free energy change of an NADH mediated reduction of acetaldehyde to ethanol if blood ethanol is 0.2% by volume, and [Acetaldehyde] = 9uM. Assume the ratio of NAD/NADH is the same as discussed in class.Based on the action of thiamine pyrophosphate in catalysis of the pyruvate dehydrogenase reaction, suggest a suitable mechanism for the fourth step in the pyruvate decarboxylase reaction in yeast:
- 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.Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.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.
- Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is — 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37°C.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.
- The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
