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

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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What are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
The enzyme pyruvate carboxylase is discovered in a bacterium that was thought not to contain it; in this case study, you’ll see how researchers study and characterize the enzyme, and, ultimately, show how it fits into a metabolic pathway. Following purification of the PYC enzyme by avidin-Sepharose affinity chromatography, the investigators carried out several experiments to characterize the enzyme. First, they ran samples of the enzyme on denaturing and non-denaturing gels; the results are shown in the figure to the right. In addition, they ran the protein through a calibrated gel filtration column, the results of which indicated that the PYC enzyme had a molecular weight of 540 kiloDaltons. In the figure, the rightmost column are where molecular weight standards of various sizes would occur if they’d been on the gels. The catalytic properties of the PYC enzyme were assessed following purification. The activity of the enzyme was assayed in the presence of ATP, pyruvate, bicarbonate…
Given the following equations of the line, a) determine the KM of the substrate that binds the strongest with the enzyme. b) determine which of the following substrates binds the least with the enzyme
Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.
What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?
From a series of flasks with a constant concentration of enzyme the following initial velocities weretaken, they were obtained as a function of the concentration of the substrate.a) Calculate the KM and Vmax kinetic parameters of the three forms (Lineweaver-Burk, Eadie-Hofstee, Dixon).b) Analyze which are the atypical data that cause a low correlation, which can be eliminated and explain youranswer.
1, For EACH of the following enzyme categories, (1) describe what the general function of the enzyme is; (2) identify a SPECIFIC enzyme in glycolysis that performs this function; and (3) identify the names of the organic substrate and product for the specific enzyme identified. Remember that the name of the category need not appear in the actual name of the enzyme. A. First enzyme category: kinase (answer (1), (2), and (3) B. Second enzyme category: dehydrogenase (answer (1), (2), and (3) C. Third enzyme category: isomerase (answer (1), (2), and (3)
There are six classes of enzymes, namely oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. (i) (ii) Cell disruption is one of the steps performed during enzyme production. Explain the reason of performing cell disruption in enzyme production and provide THREE (3) enzyme extraction methods for this type of enzyme. Explain the principles of gel electrophoresis as one of the methods used for enzyme purification.

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