Please answer asap and in short and content should not be palgarised please Complete the following table by indicating the appropriate enzyme FULLnames (from 1 to 4) affected by each allosteric effector in citric acid cycle, writedown (+) for activator and (-) for inhibitor function of effector (from a to d).Allosteric effectorEffected Enzyme in citric acid cycleEffect (+ or - )ADP1)a)АТРb)3)PyruvateSuccinyl CoA4)d)2)

The Krebs cycle (citric acid cycle) carry out the complete oxidation of acetyl CoA produced as the…

Answered: Complete the following table by…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.
Consider the following interconversion, which occurs in glycolysis :(a) What is ΔG′° for the reaction ( K'eq measured at 25 °C)?(b) If the concentration of fructose 6-phosphate is adjusted to 1.5 M and that of glucose 6-phosphate is adjusted to 0.50 M, what is ΔG?(c) Why are ΔG′° and ΔG different?
Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)
a. Arachidic acid is shown in the diagram below. How many rounds of β-oxidation will be needed to fully catabolize arachidic acid? b. What products will be obtained from the complete β-oxidation of arachidic acid? c. What will be the final ATP output (after TCA cycle and oxidative phosphorylation) obtained from the complete β-oxidation of arachidic acid?
Certain microorganisms with a modified citric acid cycle decarboxylate a-ketoglutarate to produce succinate semialdehyde: (a) Succinate semialdehyde is then converted to succinate, which is furthermetabolized by standard citric acid cycle enzymes. What kind of reactionis required to convert succinate semialdehyde to succinate? Showany coenzymes that might be involved.(b) Based on your answer in part a, how does this pathway compare to thestandard citric acid cycle in energy yield?
The malaria parasite Plasmodium falciparum does not carry out oxidative phosphorylation and therefore does not use the citric acid cycle to generate reduced cofactors. Instead, the parasite converts amino acid–derived α ketoglutarate to succinate. Write an equation for the α-ketoglutarate → succinate conversion that follows (a) the oxidative (clockwise) path of the citric acid cycle or (b) the reductive (counterclockwise) path of the cycle.
Please explain part b
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?
The half-reactions involved in the lactate dehydrogenase (LDH) reaction and their standard reduction potentials are (see attached)). Calculate ΔG at pH 7.0 for the LDH-catalyzed reduction of pyruvate under the following conditions: (a) [lactate]/[pyruvate] = 1 and [NAD+]/[NADH] = 1. (b) [lactate]/[pyruvate] = 160 and [NAD+]/[NADH] = 160. (c) [lactate]/[pyruvate] = 1000 and [NAD+]/[NADH] = 1000. (d) Discuss the eff ect of the concentration ratios in Parts a–c on the direction of the reaction.
Consider a series of experiments in which 32P-labeled inorganic phosphate were introduced to erythrocytes (red blood cells) undergoing glycolysis. Would you expect to see the labeled phosphate in any glycolytic intermediates? If so, which and at what relative concentrations?
In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.
Please explain each part thoroughly with explanations and answers given. This is Bipchemistry

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