Please write out this mechanism the formation of fructose 1,6-bisphosphate from dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3 - phosphate (GAP) catalyzed by aldolase

How many ATP are produced from the complete degradation of 1,3-bisphosphoglycerate? the complete degradation of ONE glucose using the malate-aspartate shuttle as your guide.

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.

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?

phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucitol-1,6-diphosphate. (a)  Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of substrate concentration to show a sigmoidal or hyperbolic curve? (b)  How would each of the regulators above affect the dynamics of the T state to R state equilibrium of phosphofructokinase? Briefly explain your reasoning. (c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP, AMP, and 2,5-anhydro-D-glucitol-1,6-diphosphate? Briefly explain your answers.

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

Some bacteria catabolize glucose by the Entner–Doudoroff pathway, a variant of glycolysis in which glucose-6-phosphate is converted to 6 phosphogluconate (as in the pentose phosphate pathway) and then to 2 keto-3-deoxy-6-phosphogluconate (KDPG). Next, an aldolase acts on KDPG. (a) Draw the structures of the products of the KDPG aldolase reaction. (b) Describe how these reaction products are further metabolized by glycolytic enzymes. (c) What is the ATP yield when glucose is metabolized to pyruvate by the Entner–Doudoroff pathway? How does this compare to the ATP yield of glycolysis?

Which of the following glycolytic enzymes catalyzes the conversion of fructose-1,6-bisphosphate into the two product molecules dihydroxyacetone phosphate, and glyceraldehyde-3-phosphate? phosphoglycerate kinase pyruvate kinase malate dehydrogenase aldolase phosphofructokinase

Glucagon secretion inhibits intracellular acetyl-CoA carboxylase activity through a number of different methods. Make a list of everything that comes to mind.

Refer to Figure, which indicates ΔG 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?