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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Similar questions

Which of the following statement about the enzyme thermodynamics is TRUE? a. Enzymes increase the activation barrier (∆G cat) of the products b. Enzymes decrease the activation barrier (∆G cat) of the products c. Enzymes decrease the free energy (∆G) of the products d. Enzymes decrease the free energy (∆G) of the reactants e. Enzymes increase the activation barrier (∆G cat) of the reactants
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.
What is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substrate
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 =
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
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 run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?
There is an enzyme inhibition mechanism that is not too detrimental when viewed from the size of Km, namely the inhibition mechanism.... A. non-competitiveB. non-competitive and uncompetitiveC. in-competitive and uncompetitiveD. in-competitiveE. uncompetitive
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.
Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
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?

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