AP BIO Topics 3.1 - 3.3 Enzymes

Front

What is a competitive inhibitor?

Back

A competitive inhibitor is a substance that binds to the active site of an enzyme, competing with the substrate for binding and thus reducing the rate of the reaction.

Front

What are enzymes made of?

Back

Enzymes are primarily made of proteins, which are macromolecules composed of amino acids.

Front

Does an increase in heat always denature an enzyme?

Back

False. While high temperatures can denature enzymes, moderate increases in heat may enhance enzyme activity up to a certain point.

Front

What is the primary function of an enzyme?

Back

The primary function of an enzyme is to speed up a chemical reaction by lowering the activation energy required.

Front

How can the effects of a competitive inhibitor be overcome?

Back

The effects of a competitive inhibitor can be overcome by increasing the concentration of the substrate (reactants).

Front

What is the role of the active site in an enzyme?

Back

The active site is the specific region of an enzyme where the substrate binds and the reaction occurs.

Front

What is enzyme specificity?

Back

Enzyme specificity refers to the ability of an enzyme to select and catalyze a specific substrate among many possible candidates.

Front

What factors can affect enzyme activity?

Back

Factors that can affect enzyme activity include temperature, pH, substrate concentration, and the presence of inhibitors or activators.

Front

What is a noncompetitive inhibitor?

Back

A noncompetitive inhibitor is a substance that binds to an enzyme at a site other than the active site, reducing the enzyme's activity regardless of substrate concentration.

Front

What is the significance of enzyme concentration?

Back

The concentration of enzymes affects the rate of reaction; higher enzyme concentrations generally lead to increased reaction rates, provided there is enough substrate.