False

True

True

False

It is numerically equal to the substrate concentration required to reach half maximal velocity for an enzyme-catalyzed reaction.

It has units of concentration.

It is a measure of the rate of a catalytic process.

It is a measure of enzyme efficiency.

It is numerically equal to the affinity between the enzyme and its substrate.

True

False

False

True

Adding more inhibitor should get the reaction up to speed again.

Adding more substrate will increase the rate of reaction.

The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.

Removing the irreversible inhibitor should get the reaction working again.

Add more inhibitor to speed up the reaction.

Add more substrate; it will outcompete the inhibitor and increase the reaction rate.

Increase the temperature.

Increase the pH.

False

True

Irreversible inhibitors, primarily because they covalently modify an enzyme, are often toxic.

Competitive inhibitors bind at a different site than substrate, altering the ability of the enzyme to bind its native target.

Uncompetitive inhibitors bind at a different site than substrate but only after enzyme has bound its native target.

Noncompetitive inhibitors bind at a different site than substrate, altering the ability of the enzyme to bind its native target.

A competitive inhibitor does not affect Vmax.

An uncompetitive inhibitor will always bind at the active site.

A competitive inhibitor binds irreversibly to the enzyme at the active site.

Reversible inhibitors bind to either free enzyme or the enzyme-substrate complex but not both.

An uncompetitive inhibitor typically affects KM but not kcat.

False

True

Substrate analog

Allosteric effector

Regulatory protein

Protein kinase