Why is vmax and km important

That the enzyme requires a large amount of substrate to become saturated. The enzyme has a low affinity for its substrate. Correct answer: That the enzyme requires only a small amount of substrate to become saturated.

Explanation : In enzyme kinetics, is the concentration of substrate which allows the enzyme to reach maximum reaction velocity. Example Question 5 : Vmax And Km. Possible Answers: Not enough information is given to predict.

Correct answer:. Explanation : The Michaelis constant, , is a frequently used value in enzyme kinetics used to essentially describe how much substrate is needed to speed up a reaction. Example Question 6 : Vmax And Km. Y-intercept on a Lineweaver-Burk plot. Possible Answers: I only.

Correct answer: I and II. Explanation : can be defined as or as. Example Question 7 : Vmax And Km. Possible Answers: will decrease. Correct answer: will increase. Explanation : Competitive inhibitors will block the active site of the enzyme. Copyright Notice. View Biochemistry Tutors. Rajappa Certified Tutor. University of Madras, Bachelor of Science, Chemistry. Rana Certified Tutor. Tomoe Certified Tutor. Report an issue with this question If you've found an issue with this question, please let us know.

Do not fill in this field. Louis, MO Or fill out the form below:. Company name. Copyright holder you represent if other than yourself. I am the owner, or an agent authorized to act on behalf of the owner of an exclusive right that is allegedly infringed. I have a good faith belief that the use of the material in the manner complained of is not authorized by the copyright owner, its agent, or the law.

This notification is accurate. I acknowledge that there may be adverse legal consequences for making false or bad faith allegations of copyright infringement by using this process. Find the Best Tutors Do not fill in this field. Your Full Name. Phone Number. Zip Code. Track your scores, create tests, and take your learning to the next level! A At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration.

The catalytic site of the enzyme is empty, waiting for substrate to bind, for much of the time, and the rate at which product can be formed is limited by the concentration of substrate which is available.

B As the concentration of substrate increases, the enzyme becomes saturated with substrate. As soon as the catalytic site is empty, more substrate is available to bind and undergo reaction. The rate of formation of product now depends on the activity of the enzyme itself, and adding more substrate will not affect the rate of the reaction to any significant effect. The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction, Vmax.

The relationship between rate of reaction and concentration of substrate depends on the affinity of the enzyme for its substrate. This is usually expressed as the Km Michaelis constant of the enzyme, an inverse measure of affinity. For practical purposes, Km is the concentration of substrate which permits the enzyme to achieve half Vmax.

An enzyme with a high Km has a low affinity for its substrate, and requires a greater concentration of substrate to achieve Vmax. The Km of an enzyme, relative to the concentration of its substrate under normal conditions permits prediction of whether or not the rate of formation of product will be affected by the availability of substrate.

From the graph find the maximum velocity and half it i. Draw a horizontal line from this point till you find the point on the graph that corresponds to it and read off the substrate concentration at that point. This will give the value of Km. Sign up now. Determining Km and Vmax.