Enzymes & Catalysis
Enzyme Kinetics
Enzyme Inhibition
Energy Carriers
Miscellaneous
100

What molecule does an enzyme bind and convert into product?

The substrate

100

What does Vmax represent in enzyme kinetics?

The maximum reaction rate of an enzyme-catalyzed reaction.

100

What type of inhibitor competes directly with the substrate for the enzyme’s active site?

A competitive inhibitor.

100

What molecule is the primary carrier of high-energy phosphate groups in cells?

ATP

100

What is oxidation?

Loss of electrons

200

What energy barrier do enzymes lower to speed up chemical reactions?

Activation energy

200

What is Km?

The substrate concentration at which the reaction rate is half of Vmax.

200

What type of inhibitor binds to an enzyme at a site other than the active site?

A noncompetitive inhibitor.

200

Which energy carrier primarily supplies high-energy electrons for biosynthesis?

NADPH

200

What is reduction?

Gain of electrons


300

What aspect of a reaction do enzymes NOT change, even though they increase reaction rate?

The equilibrium point.

300

What does a low Km indicate about an enzyme?

High affinity for its substrate.

300

Which type of inhibition increases Km but does not change Vmax?

Competitive inhibition.

300

Which carrier is most commonly associated with energy extraction during metabolism?

NADH

300

How does a competitive inhibitor impact the Km and Vmax?

does not change the Vmax, but shifts the Km to the right

400

Enzymes lower the activation energy of both the forward and reverse reactions by how much? (same or which one more?)

By the same amount.

400

Why does increasing substrate concentration eventually stop increasing reaction rate?

The enzyme has reached Vmax.

400

Which type of inhibition decreases Vmax but does not change Km?

Noncompetitive inhibition.

400

In what form do activated carrier molecules store energy?

As transferable chemical groups or high-energy electrons.

400

How does a non competitive inhibitor impact the Vmax and Km of a graph?

Vmax decreases, Km does not change

500

Why do cells break down glucose through many enzyme-catalyzed steps instead of one large reaction?

To capture energy for chemical work rather than losing it as heat.

500

Two enzymes have the same Vmax, but enzyme A has a lower Km than enzyme B. Under what condition will enzyme A reach a higher reaction rate?

At lower substrate concentrations.

500

Which type of inhibition can be overcome by increasing substrate concentration?

Competitive inhibition.

500

ATP hydrolysis is most often coupled to what type of reaction in biosynthesis?

Condensation reactions

500

Explain both competitive and noncompetitive inhibition.

Competitive: competes with substrate for binding to the enzyme active site

Noncompetitive: binds enzyme (not active site) to inhibit the enzyme activity and changes the active site.

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