2. The two diagrams to the right il-lustrate plots of steady-state ki-netic studies to characterize the in-teraction of heart muscle phos-phofructokinase-1 with a non-phy-siological, synthetic substrate fruc-tose-6-sulfate. Because the kcat issmaller than that for the natural50.8-NH =3.50.6-0.4-0.2-10 μΜ20 μΜ48 µMsubstrate, higher enzyme concen-trations could be used. The resultsshow the influence of increasing20.2-0.4-concentrations of ATP on the initial-0.6->velocity of the enzyme catalyzedreaction in the presence of no-0.8F41220283644526068768492.22.02.4ΑMP () , 10 μΜ AMP (+ ) 20 μΜAMP (-), and 48 µM AMP (-).[AΤP] (μΜ)log[ATP] (µM)(a) .Write the reaction in words catalyzed by the enzyme for the alternative substrate, describehow ATP interacts with the enzyme in the case of no AMP (•).(b) !with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme.Explain the physical significance of the displacement of the Hill plots to the right in panel B10 (µmoles/min/mg)A (A - "A) boj

Phosphofructokinase adds a phosphoryl group from ATP to Fructose 6 phosphate (F6P) to yield Fructose…

Answered: 2. The two diagrams to the right il-…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 17P

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An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare
1E In terms of binding adenylate kinase, the Kd for ATP is ~50 M and the KI for GMP-PCP is ~50 nM. Explain how this may be possible in terms of molecular interactions. Name 4 different types of molecular interactions that may contribute to the increased binding affinity exhibited by GMP-PCP. Please help me in details
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.
At 37 °C, the serine protease subtilisin has kcat = 50 s-1 and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes ahydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415–423) the following kinetic parameters for the N155T mutant of subtilisin: kcat = 0.02 s-1 and KM = 2 × 10-4 M.(a) Subtilisin is used in some laundry detergents to help remove protein-type stains. What unusual kind of stability does this suggest for subtilisin?(b) Subtilisin does have a problem in that it becomes inactivated by oxidation of a methionine close to the active site. Suggest a way to make abetter subtilisin.(c) Is the effect of the N155T mutation what you would expect for a residuethat makes up part of the oxyanion hole? How do the reported values ofkcat and KM support your answer?(d) Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize…
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
Inhibition of Purine and Pyrimidine Metabolism by Pharmacological Agents Indicate which reactions of purine or pyrimidine metabolism are affected by the inhibitors (a) azaserine, (b) methotrexate, (c) sulfonamides, (d) allopurinol, and (e) 5-fluorouracil.
One can identify phenylketonurics and PKU carriers (heterozygotes) by means of a phenylalanine tolerance test. One injects a large dose of phenylalanine into the bloodstream and measures its clearance from the blood by measuring serum phenylalanine levels at regular intervals. Sketch curves showing relative blood phenylalanine concentration versus time that you would expect to be displayed by (a) a PKU patient, (b) a heterozygote, and (c) a normal individual. What kind of tolerance test could you devise to distinguish between PKU resulting from either phenylalanine hydroxylase deficiency or dihydropteridine reductase deficiency?
A variant of hemoglobin (Boston variant; mutation His E7(58)α → Tyr) promotes methemoglobin formation involving the α (alpha) subunits. What is the maximum value of the Hill constant (n) that you could measure for the Boston variant of hemoglobin? log (YO2 / 1 - YO2 ) = log pO2 - logP50 Please break down each step of the Hill equation and explain why the result for n is valid from a logical standpoint.
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
6. If inhibitor X changes lactase activity to a Vo of 0.333333333333 mM per minute when [S] = 2.0 mM, and a Vo of 0.50 mM per minute when [S] = 3.33333333333 mM, calculate the new Vmax. 1.0 mM per minute 2.0 mM per minute 2.5 mM per minute 5.0 mM per minute 10.0 mM per minute 7. Calculate the new Km of the lactase reaction with inhibitor X. 1.0 mM 2.0 mM 2.5 mM 5.0 mM 10.0 mM 8. Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. 1.0 per minute 2.0 per minute 2.5 per minute 5.0 per minute 10.0 per minute Inhibitor X exerts which of the following effects on the above enzyme (lactase)? uncompetitive inhibition mixed noncompetitive inhibition competitive inhibition pure noncompetitive inhibition all of the above
The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.

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