4. Aerobic respiration of 5 mM acetate solution. Assume no other carbon source and that acetate is equivalent to acetyl-CoA. NADH FADH2 OP ATP SLP ATP Total ATP Show your work using dimensional analysis here: 5. Aerobic respiration of 2 mM alpha-ketoglutaric acid solution. Assume no other carbon source. NADH FADH2 OP ATP Show your work using dimensional analysis here: SLP ATP Total ATP

4. Aerobic respiration of 5 mM acetate solution. Assume no other carbon source and that acetate is equivalent to acetyl-CoA. NADH FADH2 OP ATP SLP ATP Total ATP Show your work using dimensional analysis here: 5. Aerobic respiration of 2 mM alpha-ketoglutaric acid solution. Assume no other carbon source. NADH FADH2 OP ATP Show your work using dimensional analysis here: SLP ATP Total ATP

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 22P: Based on your residing of this chapter, what would you expect to be the most immediate effect oil...

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Characterizing Glycolysis List the reactions of glycolysis that a. are energy consuming (under standard-stale conditions), b. are energy yielding (under standard-state conditions), c. consume ATP. d. yield ATP e. are strongly influenced by changes in concentration of substrate and product because of their molecularity. f. are at or near equilibrium in the erythrocyte (see Table 18.2).
Comparing Glycolysis Entry Points for Sucrose Sucrose can enter glycolysis by either of two routes: Sucrose phosphorylase: Sucrose + Pi fructose + glucose-1-phosphate Invertase: Sucrose + H20 fructose + glucose Would either of these reactions offer Jin advantage over the other In the preparation of hexoses fur entry into glycolysis?
Effects of Changing Metabolite Concentrations on Glycolysis In an erythrocyte undergoing glycolysis what would be the effect of a sudden increase in the concentration of a. AÎ¤P? b. AMP? c. fructose-1.6-bisphosphate? d. fructose-2, 6-bisphosphate? e. citrate? f. glucose-6-phospthate?
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?
Radiotracer Labeling of Pyruvate from Glucose Determine the anticipated location in pyruvate of labeled carbons If glucose molecules labeled (in separate experiments.) with 14C at each position of (.tie carbon skeleton proceed through the glycolytic pathway.
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.
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.
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.
Complete oxidation of a 16-carbon fatty acid can yield 129 molecules of ATP Study Figure 19.2 and determine how many ATP molecules would be generated if a 16-carbon fatly acid were metabolized solely by the TCA cycle, in the form of S acetyl-CoA molecules.
Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have serious consequences for humans For example, defects in the gene for pyruvate kinase can result in a condition known as hemolytic anemia. Consult a reference to learn about hemolytic anemia, and discuss why such genetic defects lead to this condition.
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.
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.