1The carbon skeletons of amino acids can be catabolised via various steps. These end products areoften intermediates of the citric acid cycle.100X0 0801For example:Valine →→→succinyl-CoAArginine →→→ a-ketoglutarateAspartate →→→→ oxaloacetateWhat is the theoretical ATP yield from the catabolism of the end product of valine degradation feedinginto the citric acid cycle?OND OND(Your answer should consider ATP production from the citric acid cycle up until oxaloacetate, as well aselectron transport chain-mediated production of ATP. Your answer should be a number, without anyother text. E.g.: 2. The image below has been provided to help you.):00:0Acetyl-CoANADHOxaloacetateMalateFumarate1.040CitrateIsocitrate*a-ketoglutaratefSuccinyl-CoACO2CO₂NADHNET16.010:00:0ONDINADH DOROHOI 1The carbon skeletons of amino acids can be catabolised via various steps. These end products areoften intermediates of the citric acid cycle.100X0 0801For example:Valine →→→succinyl-CoAArginine →→→ a-ketoglutarateAspartate →→→→ oxaloacetateWhat is the theoretical ATP yield from the catabolism of the end product of valine degradation feedinginto the citric acid cycle?OND OND(Your answer should consider ATP production from the citric acid cycle up until oxaloacetate, as well aselectron transport chain-mediated production of ATP. Your answer should be a number, without anyother text. E.g.: 2. The image below has been provided to help you.):00:0Acetyl-CoANADHOxaloacetateMalateFumarate1.040CitrateIsocitrate*a-ketoglutaratefSuccinyl-CoACO2CO₂NADHNET16.010:00:0ONDINADH DOROHOI

The Krebs cycle or Citric acid cycle occurs in the mitochondrial matrix. The cycle is never ending…

Answered: The carbon skeletons of amino acids can…

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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The inilial reactions in the biosynthesis of the amino acid aspartate at 298 K are: Carbamoyphoephate Cartamoyi + phosphate ADP + phoaphate - ATP AO=-12,300 calmol AG-T800 calimol Which of the following statements is gorrect? A) The energy which is released fron the conversion of 1 mole of carbamoyphosphate to carbamoyl+ phosphate (P) in reaction I is sufficient to drive the synthesis of 1 mole of ATP in reaction II. B) AG for the reaction Carbamoyphosphate + Carbamoyl + phosphate is +123 kcalimol. c) AHP for reaction I cannot be detemined trom the information given. D) Al of the above. E) None of the above.
Two pathways that yield NADPH in the cytosol, needed for fatty acid biosynthesis, are: (1) (2) The correct repeated sequence of 4 types of chemical reactions involved in the fatty acid biosynthesis are: (1) , (2) (3) (4) Which molecule allosterically activates the rate-limiting enzyme of the fatty acid biosynthesis? Tor F Mammals can synthesize 18:3 (469.12) from, 18:2 (4¹2) What is the source of methyl group in the formation of phosphatidylcholine from phosphatidylethanolamine? and In mammals (strategy-II), phosphatidylcholine is yielded by the condensation of these two molecules. The two precursors for the synthesis of sphingosine in sphingolipids are:
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.
Drawthe structures of the two citric acid cycle intermediates that can be converted into amino acids in a single step by transamination. What amino acids do they produce?Draw their structures.
Starch synthase in plants contains a single active site that accommodatesADP–glucose. However, cellulose synthase may contain two UDP–glucose-binding active sites. Given the structural diff erences between starch and cellulose, explain why two substrate-binding sites would promote effi cient cellulose synthesis.
In addition to consumption by glycolysis, glucose 6-phosphate is used to generate other 5. (a) key cellular metabolites – including precursors for nucleic acids and modulators of cellular red/ox bal- ance – via the oxidative phase of the pentose phosphate pathway. What nucleic acid precursor mole- cule and what key cofactor are generated by the oxidative phase of the pentose phosphate pathway? Draw the reactions including all reactants and products that comprise this phase of the pathway.
(b) ☐ The exergonic reactions catalyzed by isocitrate dehydrogenase (ICDH) and α- ketoglutarate dehydroge-nase (aKGDH) are regu- lated by metabolites, in addition to the reaction catalyzed by citrate synthase. The diagram to the right illustrates the activity of ICDH (A,▲) and aKGDH (O,●) in the presence of 1.5 mM ADP (O,A) or 1.5 mM ATP (●,▲). In muscle tissue contraction of sarcomeres initiated by a nerve im- pulse results first in the release of Ca 2+ from the sarcoplasmic reticulum. As indicated by the chang- es in velocity of the two enzymes, what are the flux changes of the TCA cycle in muscle tissue upon release of Ca2+ under the influence of ADP viz. ATP and under the influence of NAD+ viz. NADH on cit- rate synthase? 100 75 Stimulation of activity (% of maximum) ŏ 25 1. -8 -7 -6 log {[Ca2+] (M)}
Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?(notice that its 450 kj not 450j)
Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain? Please be aware that energy is 450 kJ.mol-1, not 450 J.mol-1
Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 kJ.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain? (notice that its 450 kj not j)
. Because of the position of arsenic in the periodic table, arsenate (AsO}-) is chemically similar to inorganic phosphate and is used by phosphate-requiring enzymes as an alternative substrate. However, organic arsenates are quite unstable and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.
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?Do a bit or research on the structure one of these enzymes. (include one recent reference) – How detailed is the enzyme structure known? What insight(s) does this structural detail give you about the enzyme mechanism.

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