which statements are False In the TCA Cycle 3 molecules of NADH are produced per molecule of Acetyl-CoA oxidizedaIntracellular concentrations in resting muscle are as follows: Fructose-6-phosphate (1.0 mM)Fructose-(1-6)-bisphosphate (10.0 mM)AMP (0.1 mM)ADP (0.5 mM)bАТР (5.0 mM)Pi (10.0 mM)Under the above conditions the Phosphofructokinase reaction in muscle is more exergonic than under standardconditions.The E2 component of the Pyruvate Dehydrogenase complex binds NAD* in its active site.If 1co2 was bubbled through a suspension of liver cells that was undergoing gluconeogenesis from lactate to glucosecarbons 1 and 6 of glucose would be radioactiveWhen Acetyl-CoA levels exceed the Oxaloacetate supply allosteric activation of Pyruvate Carboxylase the Acetyl-CoA raisesthe Oxaloacetate levels for condensation with Acetyl-CoA to form CitrateeThe carbon atom of the -CO0 group attached to the keto carbon of Oxaloacetate is released as carbon dioxide in thefIsocitrate Dehydrogenase reactionThe two electrons derived from the Pyruvate Dehydrogenase complex come from dihydrolipoic acidThe reaction of Malate oxidation to Oxaloacetate occurs because Oxaloacetate is used in the next reaction which has ahnegative AGThe only reaction of the Citric Acid Cycle that provides substrate level phosphorylation is catalyzed by Succinyl CoAiSynthetaseb0

Glucose is the ultimate source of energy for humans which is metabolized and converted into pyruvate…

Answered: which statements are False

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

See similar textbooks

Similar questions

How much ATP is produced from the complete B-Oxidation of myristic acid (C14H2802)? Activation of Fatty Acid ACCOA x (10 ATP/ACCOA) FADH₂ x (1.5 ATP/FADH₂) = NADH x (2.5 ATP/NADH) : = = -2 ATP ATP ATP ATP TOTAL ATP C18 CH, (CH₂)₁4-CH₂-CH₂-C-S-COA || FAD →FADH₂ CH₂(CH₂)₁4-CH=CH-C-S-CoA Each loop of the pathway represents a repetition of Steps 1-4. H₂O OH CH₂(CH₂)₁4-CH-CH₂-C-S-CoA || - NAD+ →→NADH+ H 0 CH3-(CH₂) 14 C-CH₂-C-S-CoA 0 || C16 CH₂(CH₂)14-C-S-CoA COA-SH Acyl CoA trans-Enoyl COA L-B-Hydroxyacyl CoA B-Ketoacyl COA H₁-C-S- + CH₂-C-S-CoA Acetyl CoA New acyl COA C₁4+ Acetyl CoA C12+ Acetyl CoA CO+ Acetyl CoA Cg+ Acetyl CoA C + Acetyl COA C₁ + Acetyl COA 2 Acetyl COA
10 ATP/Acetyl-CoA * 2 acetyl-CoA = 20 ATP 1 GTP/ Acetyl-CoA * 2 acetyl-CoA = 2 GTP 1,5 ATP/ FADH2 * 1 FADH2= 1,5 ATP 2,5 ATP/ NADH * 3 NADH = 7,5 ATP 7,5 + 1,5 + 20 = 29 ATP och 2 GTP All of this is round off, how to calculate without rounding off? 2-Acetyl-CoA and 15 subunits
The glutamate dehydrogenase (GDH) catalyses the following reaction: H +H₂N- -C -COO CH₂ CH₂ COO™ acide glutamique + NAD + H₂O GDH Time (min) A340 COO™ c=o CH₂ 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ COO + NH4+ NADH + H+ acide a-cétoglutarique The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm7 6 7 8 9 10 1.550 1.510 1.489 1.476 1.451 Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. proteins - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. -…
The transformation of glucose to lactate in myocytes releases only about 7% of the free energy released when glucose is completely oxidized to CO2 and H2O. Does this mean that anaerobic glycolysis in muscle is a wasteful use of glucose? Explain.
Assuming that the glycerol 3-phosphate shuttle is operative, a complete oxidation of three molecules of glucose (by a eukaryotic cell) into carbon dioxide and water would produce approximately ATP molecules via oxidative phosphorylation only. (Consider NADH = 2.5 ATP and FADH2 = 1.5 ATP)
Net moles of ATP produced by one mole of acetyl CoA entering the TCA cycle is: 9 38 4
Phosphofructokinase-1 is the main flux controlling enzyme for glycolysis. It is inhibited by high [ATP]. There exist metabolic circumstances in which the inhibition by ATP is overridden. Draw velocity vs. [S] graphs showing the inhibition of PFK-1 activity by ATP and the circumstance in which the inhibition by ATP is overridden.
phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucitol-1,6-diphosphate. (a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of substrate concentration to show a sigmoidal or hyperbolic curve? (b) How would each of the regulators above affect the dynamics of the T state to R state equilibrium of phosphofructokinase? Briefly explain your reasoning. (c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP, AMP, and 2,5-anhydro-D-glucitol-1,6-diphosphate? Briefly explain your answers.
The enzyme lactate dehydrogenase catalyzes the reversible reaction lactate (CH3 CHOHCOO )+NAD* рyruvate (CH3 COCOO) + NADH + H+ Given the standard reduction potentials CH3 СОСОО + 2H+ + 2е CH3 CHОНСО" E°'= -0. 185 V NADŤ + H+ + 2e- → NADH = -0. 320 V E°' would you expect the reaction to be spontaneous in the forward or reverse direction under biochemical standard state conditions? How could you change the reaction conditions to force the reaction to be spontaneous in the opposite direction? Please explain your answer.
Which of the following is higher during high levels of glutathione reductase and NADP? SH A но (GSH) OH NH2 NH2 HO OH ;-CH-CH2-CH2-C-NH-CH–ċ–NH–CH2- CH2 В (GSSG) CH2 -CH-CH;-CH2=C-NH–C NH-CH–Ç-NH-CH2-C HO OH NH2
Write out the balanced chemical equation for the oxidation of C16:cis-9 to acetyl-CoA, including electron transfers and oxidative phosphorylations (ATP). (Convert the NADH & FADH2 to ATP) 1 FADH2 = 1.5 ATP 1 NADH = 2.5 ATP
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?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS