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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Which of the following is NOT true? a. For many enzymes, Vmax is essentially equal to k3. b. Km is the reaction rate at 1/2 Vmax. c. At steady state the formation of ES is equal to the breakdown of ES. d. A Lineweaver-Burke plot generates a straight line. e. An Eadie-Hofstee plot generates a straight line.
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. A competitive inhibitor would bind at the enzyme's active site.B. As a result, the affinity of the substrate to the active site decreases.
A biochemist wants to determine the effect of an inhibitor on a certain enzyme. The data are shown below: Vo (mM/min) (without inhibitor) Vo (mM/min) (with inhibitor) [Substrate] (mM) 15 1.11 0.67 30 1.81 1.17 45 2.28 1.56 60 2.62 1.88 90 3.09 2.36 Using linear regression analysis, determine the values of Vmax and Km of the enzyme in the ab- sence of an inhibitor. - y-int = - slope = - vmax = - Km =
In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm
A biologist investigating enzyme function plotted the activity of a particular enzyme (y-axis) vs pH (x-axis). Experiment A was performed at 30 oC, experiment B at 10 oC and experiment C at 100 oC. Experiments A, B, and C all used the same type of enzyme, they simple tested the enzyme's activity at different temperatures. Using your knowledge of enzyme activity, answer the questions based on the results shown in the graph. (Answer question B) Graph included B. Why is there no hill in the middle of line C?
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
Given the parameters below:1. u(max) = 1.0/ h Ks = 10 uM2. u(max) = 0.7/h Ks = 2 uM) a. sketch the comparative Substrate Concentration vs.u(max) graphs for 1. b. sketch the comparative Substrate Concentration vs.u(max) graphs for 2. (answer a and b)
Which of the following statements about enzyme regulation is NOT true? a. covalent modification is one type of enzyme regulation. b. biologically most important type of regulation is standard inhibition. c. allosteric regulation can involved feedback inhibition. d. some types of enzume regulation are not widely used in biology. e. none of the above
Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
You put 50 uL of 0.1 mg of protein into a 1 cm pathlength cuvette containing 3 mL of LDH reaction mixture and measure a slope of 0.125 abs/min in an LDH assay. What is the specific activity of the enzyme sample? Show your work.
Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share the same value for Vmax. Using this information, can you derive conclusions how the km values for enzymes A and B compare to each other?
An uncatalyzed reaction has a rate of 6.2x10-7 sec-1. When an enzyme is added the rate is 1.2x104 sec-1. Calculate rate of enhancement caused by enzyme. Options are: A. 1.9x1010 B. 5.2x10-11 C. 7.4x10-3 D. The data are not appropriate for calculation requested. E. 1.2x104

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