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Enzyme Kinetics

Authored by Shelby Thompson

Biology

University

NGSS covered

Used 1+ times

Enzyme Kinetics
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74 questions

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1.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the primary reason an enzyme can increase the rate of a chemical reaction?

It lowers the activation energy required for the reaction.

It increases the temperature of the reaction.

It changes the products of the reaction.

It adds more reactants to the reaction.

Tags

NGSS.HS-PS1-5

2.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

Which of the following best describes the active site of an enzyme?

The region where substrate molecules bind and undergo a chemical reaction.

The part of the enzyme that is released after the reaction.

The area where cofactors are stored.

The site where inhibitors permanently attach.

3.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is a transition state in the context of enzyme-catalyzed reactions?

A high-energy intermediate state during the conversion of reactants to products.

The final product of the reaction.

The initial binding of the substrate to the enzyme.

A type of enzyme inhibitor.

Tags

NGSS.HS-PS1-2

4.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

Which statement best compares a coenzyme and a cofactor?

A coenzyme is an organic molecule, while a cofactor can be either inorganic or organic.

A coenzyme is always a metal ion, while a cofactor is always a protein.

A coenzyme is a type of enzyme, while a cofactor is not.

A coenzyme and a cofactor are both always proteins.

5.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the role of a zymogen in biochemical reactions?

It is an inactive precursor of an enzyme that requires modification to become active.

It is a type of substrate that binds to enzymes.

It is a molecule that inhibits enzyme activity.

It is a cofactor required for enzyme function.

6.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

How many classifications of enzymes are there according to the objectives listed?

6

3

4

8

7.

MULTIPLE CHOICE QUESTION

30 sec • 1 pt

What is the significance of the Michaelis-Menten equation in enzyme kinetics?

It describes the relationship between substrate concentration and reaction rate.

It measures the temperature dependence of enzyme activity.

It explains the structure of enzyme active sites.

It determines the pH optimum for enzyme function.

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