Compound X is metabolised by two distinct primary metabolicpathways. In vitro metabolism studies have found thatPathway 1 has a KM of 5 μM and a Vmax of 50 pmol/min/mgprotein, whereas Pathway 2 has a KM of 20 μM and a Vmax of5 pmol/min/mg protein.i)At a Compound X concentration of 0.1 µM, calculate the intrinsic clearancevalues for (a) Pathway 1, (b) Pathway 2, and (c) overall metabolism by thesetwo pathwaysii)At a Compound X concentration of 0.1 µM, state which is the majormetabolic pathway out of Pathway 1 and Pathway 2, and justify your answer.iii) Using the information you have been given, calculate the rate of metabolismvia Pathway 1 at a Compound X concentration of 0.1 μM.iv) Using the information you have been given, calculate the rate of metabolismdue to Pathway 2 at a Compound X concentration of 40 µMⒸ

Intrinsic clearance (Clint) is the measure of ability of hepatic enzymes to metabolize drugs. Clint…

Answered: Compound X is metabolised by two…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 4P

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The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?
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.
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
Given the following information, calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pH 7.0: [NAD+]/[NADH] = 8, [α-ketoglutarate] = 0.1 mM, and [isocitrate] = 0.02 mM. Assume standard conditions for CO2 (ΔG°′ is given in Table). Is this reaction a likely site for metabolic control?
1.1)the following data duscribe an enzyme-catalyzed reaction(hydrolysis of cabobenzoxyglycyl-L-tryptophan) Plot these results using a lineweaver-Burk method, and determine values for Km and Vmax. substrate concenrate(mM) Velocity(mM.sec-1) 2,5 0.024 5 0.036 10 0.053 15 0.060 20 0.061 25 0.062
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.
A dialyzed pigeon liver extract will catalyze the conversion of acetyl-CoAto palmitate and CoASH if supplied with Mg2+, NADPH, ATP, HCO3-, andcitrate.(a) If H14CO3– is supplied, what compounds will become labeled (permanently or transiently) during the course of the reaction? In whatcompounds will 14C accumulate?(b) Explain the role of citrate in this reaction.
Recall that beta-hydroxybutyrate is oxidized by the enzyme beta-hydroxybutyrate dehydrogenase withsimultaneous reduction of NAD+ to NADH. How might this affect the reduction potential at Complex I in theelectron transport chain? (Note: you will need to use the form of the Nernst equation that uses non-standardconditions.)
For the following aspartase reaction in the presence of the inhibitor hydroxymethylaspartate, determine Km and whether the inhibition is competitive or noncompetitive. You have to plot thegraph on the graph paper and also by using excel.[S] V, No Inhibitor V, Inhibitor Present(molarity) (arbitrary units) (same arbitrary units) 1 x 10-4 0.026 0.0105 x 10-4 0.092 0.0401.5 x 10-3 0.136 0.0862.5 x 10-3 0.150 0.1205 x 10-3 0.165 0.142
In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.
Energetics of the Hexokinase Reaction The standard-state free energy change. Gfor the hexokinase reaction, is â€” 1 6.7 kJ/mol. Use the values in Table I to calculate the value of Gfor this reaction in the erythrocyte at 37Â°C.
10a) Outline the mechanism for the conversion of alpha-ketoglutarate to succinyl-CoA which is catalyzed by alpha-ketoglutarate dehydrogenase. b) Of the five steps involved with this process, which would most likely be metabolically irreversible under physiological conditions?

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