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 toArsenate, which of the following metabolites of glycolysis will not be detectable in the cell?2-phosphoglycerateB 3-phosphoglycerateFructose 6-phosphateGlucose 6-phosphateE 1,3-bisphosphoglycerate

Glycolysis is the metabolic process in which one molecule of glucose is converted to two molecules…

Answered: Arsenate (HASO42-) can replace…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 14P

See similar textbooks

Similar questions

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.
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.
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.
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
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?
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
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
In the first stage of glycolysis, fructose-1,6-bisphosphate iscleaved to form glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. The latter molecule can then be converted to glyceraldehyde-3-phosphate. Illustrate themechanisms whereby these reactions occur
The oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate, catalyzed by glyceraldehyde 3- phosphate dehydrogenase, proceeds with an unfavorable equilibrium constant ( K'eq= 0.08; ΔG′° = 6.3 kJ/mol), yet the flow through this point in the glycolytic pathway proceeds smoothly. How does the cell overcome the unfavorable equilibrium?
ATP, like ADP and AMP, is a competitive inhibitor of NADH binding to malate dehydrogenase. Provide a structural explanation for this inhibition.
The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconcogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP] and [Pi] =1 mM. Consider the following glycolytic reaction catalyzed by hexokinase: ATP + glucose = AG' = -16.7 kJ/mol ADP + glucose-6-phosphate (a) Calculate the equilibrium constant (K) for this reaction at 298 K, and from that, calculate the maximum [glucose-6-phosphate]/[glucose] ratio that would exist under conditions where the reaction is still thermody- namically favorable. (b) The reverse of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H,0 = glucose + P, AGr = -13.8 kJ/mol K= 262 for this reaction. Calculate the maximum ratio of [glucose]/ [glucose-6-phosphate] that would exist under conditions where the reaction is still thermodynamically favorable. (c) Under what cellular conditions would both directions in the…
What if the phosphate group for the glycolysis reaction with enzyme glyceraldehyde 3-phosphate dehydrogenase was from ATP instead of Pi? What would the complete, balanced, net rxn of glycoslysisequation be and how does this impact the overall glycolysis rxn?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS