The muscle isozyme of lactate dehydrogenase is inhibited by lactate.Steady state kinetic analysis yielded the following data, with lactateeither absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in oneplot, NADH in the other. Identify each. Use an arrow and the appro-priate letter (b, c, d, or e) to identify each of the following.(b) Reciprocal of Vmax for the uninhibited enzyme.(c) The line representing data obtained in the presence of lactateacting as a competitive inhibitor with respect to the variablesubstrate.(d) The line representing data obtained in the presence of lactateacting as a mixed inhibitor with respect to the variable substrate.

Enzymes are proteinaceous substances that are capable of catalyzing chemical reactions of biological…

Answered: The muscle isozyme of lactate…

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 23P: Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the...

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The muscle isozyme of lactate dehydrogenase is inhibited by lactate. Steady-state kinetic analysis yielded the following data, with lactate either absent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot,NADH in the other. Identify each. Use an arrow and the appropriate letter(b, c, d, or e) to identify each of the following.(b) Reciprocal of Vmax for the uninhibited enzyme.(c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate.(d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate.(e) Reciprocal of KM in the presence of lactate acting as a competitiveinhibitor.(f) If KM for NADH is 2 x 10-5 M, then which of the following is the mostappropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?
The muscle isozyme of lactate dehydrogenase is inhibited by lactate.Steady-state kinetic analysis yielded the following data, with lactate eitherabsent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot, NADH in the other. Identify each. Use an arrow and the appropriate letter (b,c,d,ore) to identify each of the following. (b) Reciprocal of Vmax for the uninhibited enzyme. (c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate. (d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate. (e) Reciprocal of KM in the presence of lactate acting as a competitive inhibitor. (f) If KM for NADH is 2 x 10-5 M, then which of the following is the most appropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?M
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.
Arrange the balanced biochemical equations for all the reactions in the payoff phase of glycolysis and the conversion of pyruvate to lactate.
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Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)

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