QUESTION 17calculate the KM ANDthe total amount of enzyme present in these experiments.The following equations relate to this question. (Hint 1: some data is directly apparent without need to do calculations; Hint 2:Watch your exponents.)Kcat=Substrateconcentration(mm)12461001,000The turnover number for an enzyme is known to be 5,000 min-1. From the following set of data,250334376500500Vmax[Et]Initialvelocity(μmol/min)167G. 10 mMH. 250 uM1. 2 mMJ. 100 mMPart 1Total Enzyme amount (choose from options A-E)Part 2 (Enzyme KM: (choose from options G-J)A. Total enzyme = 10 umolB. Total enzyme = 0.1 umolOC. Total enzyme = 100 μmolD. Total enzyme = 1000 μmolE. Total enzyme = 10 μmolOFVo =Vmax[S]KM + [S]

As given in the question, Kcat (turnover number) = 5000 min-1 KM = ? Et (total enzyme concentration)…

Answered: QUESTION 17 calculate the KM AND the…

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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Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.
Question 1: ATP synthases contains 3 copies of each of the large subunits (called α and β in the E. coli enzyme). The number of c subunits can vary among different ATP synthases, ranging from 8 to 17. Part a: Briefly explain how this variation in the number of c subunits would affect the energetics of ATP synthesis. For a fixed value of the protonmotive force, how much energy can the gradient provide to drive one revolution of the ATP synthase, in a synthase with 8 c- subunits versus a synthase with 17 c-subunits?
Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.
Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
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QUESTION 2An isocitrate dehydrogenase assay was performed on the enzyme sample and found to give an absorbance change at 340nm of 0.5 absorbance units perminute. Given that the molar absorption coefficient (E) is 6220 M-1 cm-1 and the pathlength is 1cm, what is the rate of the enzyme catalysed reaction in umol perminute per mL?
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Question 1: The overall process enabled by the glyoxylate cycle is: (2acetyl-CoA) + (NAD+) + (2H2O) → (succinate) + (2CoA) + (NADH) + (2H+) Dissect this process further by writing down all of the reactions that are actually involved in making one succinate from two acetyl-CoA units. Show chemical structure for all intermediates.

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