When measuring reaction velocity as a function of substrate concentration, a researcher usuallykeeps the concentration of enzyme at a constant level. What would happen if the enzymeconcentration were not kept constant?A. Vmax would change, but Km would remain constant.B. Both Vmax and Km would changeC. Vmax would remain constant, but Km would changeD. Vmax would remain constant, but V would changeE. None of the above would necessarily occur

Michaelis- Menten equation is used to predict the rate of enzymatic reaction at different substrate…

Answered: When measuring reaction velocity as a…

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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Write Cifonly statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. When an inhibitor binds to the enzyme-substrate complex, the inhibition mode is uncompetitive. B. As a consequence, the enzyme's efficiency is decreased along with the maximum velocity.
Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?
in the concerted model of enzyme action when the L ratio (T/R) is 10,000 the velocity vs. Substrate plot results in what type of a curve.
Consider the following data set of enzymes A, B C and D which catalyze the same reaction. Enzyme A km = 5mM Vmax = 225MM/sec Enzyme B km = 50mM Vmax = 430mM/sec Enzyme C km = 15mM Vmax = 235mM/sec %3D Enzyme D km 12mM Vmax = 533mM/sec When concentrations of substrate are very low, which is the enzyme that is producing most product? MacBook Air DO F5 S0 # 12 F4 F3 %
In an experiment, three batches of the same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor. In each batch, the inhibitor was of a different type: a.Batch 1: competitive inhibitor b.Batch 2:uncompetitive inhibitor c.Batch 3:non-competitive inhibitor Assuming that Vmax = 80 mM s', Km = 8 mM, and Kiof all three inhibitors was 10 mM, which of the inhibitors was the most efficient on Vo? Explain your answer.
The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time. b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time. c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.
In Lineweaver Burk plot: O a. The slope of the plot is the Vmax/Km O b. The intercept on X-axis is 1/Km. O c. The intercept on y-axis is 1/Vmax O d. double-reciprocal plot of enzyme kinetics is generated, where 1/VO is plotted as a function [S]. O e. All answers are correct
Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. A lower Ky reflects a less efficient enzyme. B. The KM is equivalent to the substrate concentration at 50% of the reaction's velocity limit.
WriteC if only statement A is correct, H if only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An inhibitor that binds somewhere in the enzyme other than the active site is an uncompetitive inhibitor. B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases the maximum reaction velocity.
A student performed an enzyme inhibition reaction to experimentally determine the inhibitor constant of the EI complex using Dixion plot. i. The student setup two sets of experiments. Each set contained increasing concentrations of inhibitor, constant concentration of substrate and constant concentration of Alkaline phosphatase. ii. Set 1 contained lower concentration of substrate than set 2. iii. After mixing everything, he let the reaction happen for 15 minutes and measured the absorbance. iv. Then he plotted 1/v Vs 1/[I] - What error led to an unexpected graph? A) He is supposed to change the [S] within the set. B) He was not supposed to let the reaction happen for 15minutes before measuring the absorption C) He was not supposed to change the enzyme concentration within the set D) he made no errors E) his choice of X and Y axis are incorrect
Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
The initial rate for an enzyme-catalyzed reaction has been determined at several substrate concentrations. Data are as follows: [S] µmol/L V[(umol/L) min1] 5 22 10 39 20 65 50 102 100 120 200 135 If the total enzyme concentration was 1nmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? A. 175000 B. 325000 C. 900000 D. 10000 E. 375000 F. 166000 G. 3750 H. 1000000 I. 12500

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