Can someone help with this question? L-Malate + NAD⁺ ← → Oxaloacetate + NADHAbove is what i selected for the equation, but I don't know how to find ΔE'৹. Use the table below and the following information to answer questions 15-19.Standard Reduction Potential of SomeBiologically Important Half-Reactions, at pH 7.0 and 25°C (298 K)Half-reactionE" (V)2H + 2e -Crotonyl-CoA + 2H* + 2e butyryl-CoAOxaloacetate- + 2H* + 2e malate-Pyruvate + 2H* + 2e lactateAcetaldehyde + 2H* + 2eFAD + 2H* + 2e FADH,Glutathione + 2H* + 2eS+ 2H* + 2e H,SLipoic acid + 2H* + 2eNAD* + H* + 2e NADHNADP* + H* + 2e NADPHAcetoacetate + 2H* + 2e B-hydroxybutyratea-Ketoglutarate + Co, + 2H* + 2e – isocitrate2H* + 2e" H, (at pH 7)Ferredaxin (Fe*) + e ferredaxin (Fe²*)H, (at standard conditions, pH 0)0.000-0.015-0.166-0.185-0.197-0.219*→ ethanol2 reduced glutathione-0.23-0.243-0.29-0.320-0.324→ dihydrolipoic acid-0.346-0.38-0.414-0.432Source: Data mostly from Loach, PA. (1976) in Handbook of Biochemistry and Molecular Blology, 3rd edn (Fasman,G.D. ed), Physical and Chemical Data, Vel. L po. 122-130, CRC Press, Boca Raton, AL* This is the value for free FAD: FAD bound to a specific flavoprotein (for eample succinate dehydrogenase) has a d-ferent E" that depends on s protein enironments.In the tricarboxylic acid cycle, L-malate is oxidized to oxaloacetate, using NAD+ as an oxidizing agent.Using the half reactions from the given table, what is the reaction of this reduction-oxidation?Oxaloacetate + NAD+ -- L-Malate + NADHL-Malate + Oxaloacetate -→ NAD+ + NADHL-Malate + NAD* +Oxaloacetate + NADH- -L-Malate -Oxaloacetate + NAD+ + NADH What is the AE'o of the given reaction?O.0.154-0.4860.4860.154

Given Values: Standard reduction potential for the conversion of oxaloacetate to malate = -0.166 V…

In the tricarboxylic acid cycle, L-malate is oxidized to oxaloacetate, using NAD+ as an oxidizing agent. Using the half reactions from the given table, what is the reaction of this reduction-oxidation? Oxaloacetate + NAD+ –→ L-Malate + NADH L-Malate + Oxaloacetate -- NAD* + NADH L-Malate + NAD+ – → Oxaloacetate + NADH L-Malate -- Oxaloacetate + NAD+ + NADH

In the tricarboxylic acid cycle, L-malate is oxidized to oxaloacetate, using NAD+ as an oxidizing agent. Using the half reactions from the given table, what is the reaction of this reduction-oxidation? Oxaloacetate + NAD+ –→ L-Malate + NADH L-Malate + Oxaloacetate -- NAD* + NADH L-Malate + NAD+ – → Oxaloacetate + NADH L-Malate -- Oxaloacetate + NAD+ + NADH

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 16P: Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for...

See similar textbooks

Similar questions

Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
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 standard free energy change for this reaction in the direction written is +23.8 kuimol. The tabie shows the concentrations of the three intermediates in the hepatocyte of a mammal. Intermediate Concentration (M) Fructose 1.0-bisphosphate 0.000028 Gyoeraldehyde 3phosphate 0.0000068 Ditydroxyacetone phosphate 0.000032 At body temperature (37 "C). what is the actual free energy change for the reaction (in kimol) ?
Draw the structures of the following coenzyme molecules: 1. CoA-SH/Acetyl-S-CoA 2. NAD*/NADH + H* • For both: Give full name (if you copy the formula from an Internet source, please cite it properly, for example, according to the Chicago Manual of Style. • Indicate what are the chemical groups that are active in these molecules, i.e., what group participates in metabolic reactions (be aware that both molecules may be involved in both anabolic and catabolic processes). • What vitamin or vitamins will, when modified, contribute to the structure of these molecules? • Write a short, general conclusion of the importance of these two coenzymes in metabolism.
The table below shows the purification of liver lactate dehydrogenase. Purification Table of liver LDH Step Crude Extract Ammonium Sulfate DEAE-Sephadex 5'AMP-Sepharose Volume (mL) 200 100 112 40 LDH activity (Units/mL) (mg/mL) [Protein] 47.0 50.00 90.0 63.00 51.0 1.50 137.0/ 0.4 Calculate the LDH yield for the ammonium sulfate step. Provide answer to one decimal only. Show Transcribed Text this is biochemistry and the topic is protein purification could you pleaae show me the full workings even the workings for the comversions
Fatty acids are converted to their coenzyme A esters in a reversible reaction catalyzed by acyl-CoA synthetase: R-COO +ATP +COA R-C-COA +AMP + PPi a) The reaction involves two steps the first of which forms an enzyme-bound intermediate identified as the mixed anhydride of the fatty acid and AMP: R-C-O-P-O-nibose-adenine Write two chemical equations coresponding to the two steps of the reaction catalyzed by the synthetase. b) The acyl-CoA synthetase reaction as written above is readily reversible. How might the reaction be made to favor formation of fatty acyl-CoA? Write within the box. Anything outside the box will not be graded. From the
Peroxisomes have an alternative pathway for oxidizing polyunsaturated fatty acids. They contain a hydratase that converts D-3-hydroxyacyl CoA into trans Δ²- enoyl CoA. How can this enzyme be used to oxidize CoAs containing a cis double bond at an evennumbered carbon atom (e.g., the cis-Δ¹² double bond of linoleate)?
Complete the balanced equation for the overall reaction. Select answer choice in between brackets. Sucrose + [2 Pi, 4Pi]+[4 ADP, 2 ADP, 4 ATP, 2ATP]+[2 NAD+, 4 NAD+, 6 NAD+]+[H2O, 5 H2O, 3 H2O] --> [2 cirate, 2 oxaloacetate, 2 pyruvate, 2 acetyl-coA]+[4 ADP, 2 ADP, 4 ATP, 2ATP] + [2 NAD+, 4 NAD+, 6 NAD+] + [2H+, 8H+, 6 H+, 4 H+, 10 H+] Does the commercial process require aerated culture medium—that is, is this a fermentation or an aerobic process? A. a fermentation process, because A. niger cells must use O2O2 to continuously regenerate NAD+ B. an aerobic process, because A. niger cells must use O2O2 to continuously regenerate NAD+ C. a fermentation process, because A. niger cells cannot use O2O2 to continuously regenerate NAD+ D. an aerobic process, because A. niger cells cannot use O2O2 to continuously regenerate NAD+
When grown anaerobically on glucose, yeast (S. cerevisiae) converts pyruvate to acetaldehyde, then reduces acetaldehyde to Pethanol using electrons from NADH. Write the chemical equation for the reaction that reduces acetaldehyde (CH3CHO) to ethanol (CH3CH2OH). The table provides the standard reduction potential, E', of the relevant half-reactions. Half-reaction Acetaldehyde + 2 H+ + 2e¯ → ethanol NAD+ + 2H+ + 2e¯ → NADH + H+ E'° (V) -.197 -.320 Calculate the equilibrium constant, K'eq, at 25.0 °C for the reaction that reduces acetaldehyde to ethanol. K'e ×10 = eq
25. The AG" values for the two reactions are given. 1. 2. oxaloacetate + acetyl-CoA + H₂O → citrate + COASH oxaloacetate + acetate → citrate Enzymes for reactions 1 and 2 are citrate synthase and citrate lyase, respectively. Determine the AG" for the hydrolysis of acetyl-CoA acetyl-CoA + H₂O acetate + COASH + H+ plane een isoimorfbold bns (94) opg Vp1903 9911 AG¹⁰ ? AGO = -32.2 kJ/mol AG"=-1.9 kJ/mol
The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.
Behenate (C22H44O2) can be obtained by chain elongation from palmitate. How many ATP equivalents are produced in the degradation of behenate to eleven acetyl-CoA?