What is the function of glyceraldehyde 3-phosphate dehydrogenase? catalyzes the transfer of a phosphoryl group from ATP to an acceptor oxidation of the alcohol to an aldehyde dehydration and dephosphorylation of GAP hydrolysis of GAP oxidation by NAD+ and formation of acyl-phosphate
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What is the function of glyceraldehyde 3-phosphate dehydrogenase?
catalyzes the transfer of a phosphoryl group from ATP to an acceptor
oxidation of the alcohol to an
dehydration and dephosphorylation of GAP
hydrolysis of GAP
oxidation by NAD+ and formation of acyl-phosphate
Step by step
Solved in 2 steps
- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.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.Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
- 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.The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.One of the consequences of ethanol addiction is fattyliver disease, an illness in which liver cells accumulatetriacylglycerols, the esters derived from glycerol and fattyacids. Ethanol is oxidized in the cytoplasm of liver cells byalcohol dehydrogenase and aldehyde dehydrogenase to yieldacetate and 2 NADH. Acetate is then transported into themitochondrion, where it is converted to acetyl-CoA andmetabolized by the citric acid cycle. When alcohol is consumed in excessive quantities, the resulting high levels ofNADH cause metabolic abnormalities, one of which is highlevels of fatty acid synthesis. Fatty acid synthesis, also acytoplasmic process, uses acetyl-CoA as a substrate andNADPH as a reducing agent. Determine how a high level ofcytoplasmic NADH provides a source of NADPH for fattyacid synthesis.
- Using the glycerol-3-phosphate shuttle, determine how many ATP can be produced from one mole of each of the following compounds on complete oxidation?a.) Mannoseb.) Dihydroxyacetone phosphatec.) Citrated.) Malatee.) SuccinateSelect the following enzymes that utilize a mechanism where an enediol intermediate is formed. Check all that apply: a)phosphoglucoisomerase b)triose phosphate isomerase c)aldolase d) glyceraldehyde 3-P dehydrogenase e) hexokinaseWhich of the following is true about comparing the α-ketoglutarate dehydrogenase complex and the pyruvate dehydrogenase complex? Group of answer choices They catalyze reactions that produce the exact same set of products They are both dehydrogenase complexes, but have very different structures They both catalyze reactions that oxidize NADH to NAD+ They both use the same E3 enzyme component Which of the following best describes stage 2 of the citric acid cycle? Group of answer choices ATP production by the electron transport chain production of acetyl CoA regeneration of oxaloacetate release of 2 carbons as carbon dioxide
- How many ATP may be produced from 1 mole of the following compounds on complete oxidation using the glycerol-3-phosphate shuttle? COMPOUNDSa.) Mannoseb.) Dihydroxyacetone phosphatec.) Citrated.) Malatee.) SuccinateRefer 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?Which of the following statements inaccurately describes glutamate dehydrogenase? Glutamate dehydrogenase uses either NAD+ or NADP+ in a redox reaction Glutamate dehydrogenase catalyzes an oxidative deamination reaction Glutamate dehydrogenase equilibrium lies with the reductive amination of glutamate Glutamate dehydrogenase utilizes hydrolysis to release ammonium from an imine intermediate