Pls help due asap It is possible, with the use of the reactions and enzymes considered in this chapter, to convert pyruvate into a-ketoglutaratewithout depleting any of the citric acid cycle components. Write a balanced reaction scheme for this conversion.Using this reaction scheme, classify each enzyme based on whether it is required to convert pyruvate into a-ketoglutarate.RequiredAnswer BankNot required pyruvate dehydrogenase complexa-ketoglutarate dehydrogenaseTPyruvate +succinate dehydrogenasea-ketoglutarate +pyruvate carboxylase+Answer BankComplete the overall balanced equation for the conversion of pyruvate into a-ketoglutarate.CO₂ +fumarasesuccinyl CoA synthetase+H₂O →+isocitrate dehydrogenaseaconitase+3H+citrate synthasemalate dehydrogenase

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pyruvate dehydrogenase complex a-ketoglutarate dehydrogenase Pyruvate + succinate dehydrogenase a-ketoglutarate + pyruvate carboxylase + Answer Bank CO₂ + Complete the overall balanced equation for the conversion of pyruvate into a-ketoglutarate. fumarase succinyl CoA synthetase + H₂O → + isocitrate dehydrogenase aconitase +3H+ citrate synthase malate dehydrogenase

pyruvate dehydrogenase complex a-ketoglutarate dehydrogenase Pyruvate + succinate dehydrogenase a-ketoglutarate + pyruvate carboxylase + Answer Bank CO₂ + Complete the overall balanced equation for the conversion of pyruvate into a-ketoglutarate. fumarase succinyl CoA synthetase + H₂O → + isocitrate dehydrogenase aconitase +3H+ citrate synthase malate dehydrogenase

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 7P: The Effect of lodoacetic Acid on the Glyceraldehyde-3-P Dehydrogenase Reaction (Integrates with...

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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.
Because dichloroacetate inhibits the enzyme pyruvatedehydrogenase kinase, this compound has been used,with limited results, to treat lactic acidosis. The phosphorylation of the a-subunit of the pyruvate dehydrogenasecomponent of the pyruvate dehydrogenase complex bypyruvate dehydrogenase kinase causes complete loss ofenzymatic activity. Describe the theory behind the clinicaluse of dichloroacetate.
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.
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.
Catalytic mechanism of the Pyruvate Dehydrogenase Complex Match the following coenzymes with the type of reaction or catalytic steps they are associated with during the catalysis of Pyruvate transformation into Acetyl-CoA by the Pyruvate Dehydrogenase Complex: NAD+ V [Choose] formation of a low energy thioester bond decarboxylation TPP oxidation/reduction formation of a high energy thioester bond Coenzyme A [ Choose ] Lipoyl Lysine [ Choose ] FAD [ Choose ]
The same E1-Ez-E3 multienzyme structure found in the pyruvate dehydro- genase and the a-ketoglutarate dehydrogenase complexes is also used in the branched-chain a-ketoacid dehydrogenase complex, which participates in the catabolism of branched chain amino acids. Draw the reaction product when the following substrate is acted on by the branched chain a-keto acid dehydrogenase complex. H,C -C-COo- H,C
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-bisphosphoglycerate
Identify the Krebs cycle enzyme that consumes a 3-carbon substrate molecule, producing a 2- carbon product molecule (attached to acetyl-CoA), along with NADH, and one molecule of CO2. succinyl CoA synthetase a-ketoglutarate dehydrogenase pyruvate dehydrogenase isocitrate dehydrogenase malate dehydrogenase
Of the allosteric enzymes listed below, which are suppressed by NADH? Select all that apply. the pyruvate dehydrogenase complex a-ketoglutarate dehydrogenase complex U isocitrate dehydrogenase pyruvate kinase Ophosphofructokinase hexokinase Oglucokinase
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 B 3-phosphoglycerate Fructose 6-phosphate Glucose 6-phosphate E 1,3-bisphosphoglycerate
The mechanism for the conversion from alpha kytoglutarate into succinyl CoA by alpha-ketoglutare dehydrogenase is analogous to the pyruvate dehydrogenase mechanism. Draw and show the major intermediates and arrow pushing for the enzyme-catalyze process for the conversion of alpha-ketoglutarate to succinyl CoA. Note: the carbanion of thiamine pyrophosphate nucleophillically attacks C-2 of the alpha-ketoglutarate, i.e., the carbonyl carbon of that substrate.
Explain how pyruvate dehydrogenase regulated using covalent modification (E1) of pyuvate dehydrogenase complex can be (phosphorylation or dephosphorylation).