write down the balanced equation of the reaction catalyzed by the nonphosphorylating NAD+- dependent glyceraldehyde- 3-phosphate dehydrogenase and draw the substrates and products
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- In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?Consider one of the reactions of the citric acid cycle shown below Malate + NAD+ ⇆ Oxaloacetate + NADH + H+ (malate dehydrogenase) ΔG˚′ = +29.7 kJ/mol. Describe two factors that allow this thermodynamically unfavorable reaction to occur in the direction of malate to oxaloacetate.Certain microorganisms with an incomplete citric acid cycle decarboxylate α-ketoglutarate to produce succinate semialdehyde. A dehydrogenase then converts succinate semialdehyde to succinate. These reactions can be combined with other standard citric acid cycle reactions to create a pathway from citrate to oxaloacetate. Compare the ATP and reduced cofactor yield of the standard and alternate pathways.
- Some anaerobic prokaryotes reduce elemental sulfur to H2S. Assuming 100% efficiency, how much ATP could be synthesized by the oxidation of acetate by S under standard conditions?In 1937, two German biochemists published a paper proposing these reactions as part of glucose oxidation: citrate → isocitrate → α-ketoglutarate →succinate → fumarate → malate → oxaloacetate. Adding succinate, fumarate, or malate to thin slices of tissue increased oxygen consumption, supporting the hypothesis that these molecules are intermediates in the process. However, they were puzzled by the observation that these intermediates were still present in the reaction mixture at the end of the experiment. They had thought that intermediates would be consumed as they were converted to the next molecule in the pathway. What explains the observation that these intermediates were still present? a) The pathway is a cycle, constantly regenerating intermediates as glucose is broken down. b) Succinate, fumarate, and malate are not reactants but catalysts, and catalysts are not consumed in the process. c) Succinate, fumarate, and malate increase metabolism and therefore oxygen consumption,…Under anaerobic conditions, Escherichia coli synthesizes an NADH-dependent fumarate reductase rather than succinatedehydrogenase, the flavoprotein that oxidizes succinate to fumarate. a) Write an equation for the reaction catalyzed by fumarate reductase.b) NADH produced by the glyceraldehyde-3-phosphate dehydrogenase reaction is re-oxidized by reducing an organicintermediate. Rather than reduce pyruvate to lactate, anaerobic E. coli utilize fumarate reductase. However, underanaerobiosis, the activity of -ketoglutarate dehydrogenase is virtually nonexistent. Show how fumarate is formed, usinga reaction beginning with PEP and including the necessary TCA cycle enzymes.c) What is the metabolic advantage to anaerobic E. coli in using the fumarate reductase pathway rather than lactatedehydrogenase to re-oxidize NADH?
- The krebs cycle has 8 enzymes: citrate synthase, aconitase, isocitrate dehyrogenase, a-ketoglutarate dehydrogenase, succinyl –CoA synthease, succinate dehyrogenase, fumarase and malate dehyrogenase. a)Write name the cofactors required by each enzyme reaction. b)For each enzyme determine which of the following deascribes the type of reactions catalyzed: condensation (Carbon-carbon bond formation), dehydration (Loss of water), hydration (addition of water), decarboxylation (loss of CO2), oxidation-reduction; subsrate level phospohorylation; isomerization.Because of the position of arsenic in the periodic table, arsenate (AsO43- ) is chemically similar to inorganic phosphate and is used by phosphaterequiring enzymes as an alternative substrate. Organic arsenates are quite unstable, however, and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.Organisms growing anaerobically cannot perform glycolysis for long without reducing the pyruvate from glycolysis into another compound, most commonly to lactate or to ethanol plus CO2. Both of these reactions are given below in their unbalanced forms. Explain in one sentence why one of these reducing steps is needed to sustain anaerobic glycolysis.
- Arsenate (HAsO42-) can replace inorganic phosphate (Pi) in the reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase, causing Glyceraldehyde 3-phosphate to be directly converted to 3-phosphoglycerate (NADH is still formed). If a cell is expose to Arsenate, which of the following metabolites of glycolysis will not be detectable in the cell? 2-phosphoglycerate 3-phosphoglycerate Fructose 6-phosphate Glucose 6-phosphate 1,3-bisphosphoglycerateArsenate (HASO42-) can replace inorganic phosphate (Pi) in the reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase, causing Glyceraldehyde 3-phosphate to be directly converted to 3-phosphoglycerate (NADH is still formed). If a cell is expose to Arsenate, which of the following metabolites of glycolysis will not be detectable in the cell? 2-phosphoglycerate B 3-phosphoglycerate Fructose 6-phosphate Glucose 6-phosphate E 1,3-bisphosphoglycerateAlthough both hexokinase and phosphofructokinase catalyze irreversible steps in glycolysis and the hexokinase-catalyzed step is first, phosphofructokinase is nonetheless the pacemaker of glycolysis. What does this information tell you about the fate of the glucose 6- phosphate formed by hexokinase?