phosphofructokinase reaction ofFructose-2,6-bisphosphate is a regulator of both glycolysis and gluconeogenesis for theglycolysis and the fructose-1,6-bisphosphatase reaction of gluconeogenesis. In turn, the concentration offructose-2,6-bisphosphate is regulated by many hormones, second messengers, and enzymes.Classify each condition according to its effect on glycolysis and gluconeogenesisActivates glycolysis and inhibits gluconeogenesisActivates gluconeogenesis and inhibits glycolysisAnswer Bankactivation of PFK-2increased glucagon levelsincreased levels of cAMPincreased levels of fructose-2,6-bisphosphateactivation of fructose-2,6-bisphosphatase (FBPase-2)

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 11P

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Ethanol as a Source of Metabolic Energy (Integrates with Chapters 19 and 20.) Acetate produced in ethanol metabolism can be transformed into acetyl-COA by the acetyl thiokinase reaction: Acetate+ATP+CoASHacetyleCoA+AMP+PPiAcetyle-CoA then can enter the citric acid cycle and undergo oxidation to 2 CO2by this route, assuming oxidative phosphorylation is part of the process? (Assume all reactions prior to acetyl-CoA entering the citric acid cycle occur outside the mitochondrion). Per carbon atom, which is a better metabolic fuel, ethanol or glucose? That is, how many ATP equivalents per carbon atom are generated by combustion of glucose versus ethanol to CO2?
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.
Glucagon secretion causes inhibition of intracellular acetyl-CoA carboxylase activity by several mechanisms. Name all you can think of.
Glucagon secretion inhibits intracellular acetyl-CoA carboxylase activity through a number of different methods. Make a list of everything that comes to mind.
Glycogen synthase catalyzes glycogen synthesis. Determine whether each intermediate is associated with an “increase” or “decrease” and or “no effect” on the activity of glycogen synthase. Glucose 6-phosphate – cAMP –
Phosphoenolpyruvate carboxykinase (PEPCK, figure below)catalyzes first committed (rate-limiting) step in hepatic gluconeogenesis, namely the reversible decarboxylation of oxaloacetate to phosphoenolpyruvate (PEP) and carbon dioxide. This reaction can occur using either ATP or GTP as a source of the phosphate.Which following mutation can potentially improve the binding affinity of the substrate for this enzyme? a. LYS254ARG b. LYS254ASP c. ARG333GLU d. THR255GLY
The total degradation of a fatty acid with an odd number of carbons yields acetyl-CoA and another compound, X. Show the structure of X, and describe the pathway by which it is converted into a citric acid cycle intermediate, including where any cofactors participate.
A number of genetic deficiencies in acyl CoA dehydrogenases have been described. This deficiency presents early in life after a period of fasting. Symptoms include vomiting, lethargy, and sometimes coma. Not only are blood levels of glucose low ( hypoglycemia), but starvation-induced ketosis is absent. Provide a biochemical explanation for these last two observations.
The pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate to acetyl‑CoA and CO2.CO2. Multiple copies of pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3) along with five cofactors form the PDH complex. Biochemists have studied the PDH complex for decades, in part due to its interesting use of substrate channeling during catalysis. What is the benefit of substrate channeling? A. Intermediates of a multistep reaction sequence do not dissociate from the enzyme complex. B. Every intermediate or product made by the PDH complex enters the citric acid cycle as a substrate. C. The PDH complex sequesters excess substrate to use at later time. D. Reaction progress is not limited by the diffusion constant. E.The PDH active site forms in the hydrophobic core of the complex instead of a surface‑exposed region.
The pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate to acetyl‑CoA and CO2.CO2. Multiple copies of pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3) along with five cofactors form the PDH complex. Biochemists have studied the PDH complex for decades, in part due to its interesting use of substrate channeling during catalysis. What is the molecular mechanism of substrate channeling in the PDH complex? A. The swinging lipoyllysyl arm of E2 carries electrons and an acetyl group from E1 to E2. B.The active sites of E1, E2, and E3 undergo conformational changes that move products of one reaction to their next position without solvent exposure. C.Electrons and an acetyl group travel between E1 and E2 through a tunnel in E2. D. Metal ions coordinated with thiamine pyrophosphate (TPP) in E1 shield the electrons and acetyl group from scavenging by other enzymes until they reach E3.
During strenuous activity, the demand for ATP in muscle tissue is vastly increased. In rabbit leg muscle or turkey flight muscle, the ATP isproduced almost exclusively by lactic acid fermentation. ATP is formed in the payoff phase of glycolysis by two reactions, promoted by phosphoglycerate kinase and pyruvate kinase. Suppose skeletal muscle were devoid of lactate dehydrogenase. Could it carry out strenuous physical activity; that is, could it generate ATP at a high rate by glycolysis? Explain.
Discuss the regulation of fatty acid metabolism by the isozymic forms of acetyl CoA carboxylase. Explain the reciprocal control of fatty acid synthesis and degradation and the various means by which this control is achieved

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