Enzymes are biological catalysts that speed up chemical reactions in living organisms without being consumed in the process.

Enzymes are a type of sugar molecule found in cells.

Enzymes are proteins that disrupt chemical reactions.

Enzymes are harmful substances that cells need to remove.

Enzymes lower the activation energy for a reaction, allowing the reactants to change into products more efficiently.

Enzymes increase the activation energy needed for a reaction.

Enzymes alter the structure of the reactants, preventing reactions.

Enzymes work by removing energy from the reaction environment.

The active site is the specific region on an enzyme where substrate molecules bind and undergo a chemical reaction.

The active site is where enzymes store energy.

The active site is the location where enzymes are synthesized.

The active site is the area where enzymes are deactivated.

Enzyme specificity refers to the ability of an enzyme to select and catalyze only one specific substrate or a type of reaction.

Enzyme specificity means enzymes can act on any substrate.

Enzyme specificity indicates enzymes work exclusively in specific environments.

Enzyme specificity signifies enzymes are unique to each organism.

Substrates are the molecules that an enzyme acts upon during a chemical reaction.

Substrates are the products formed in an enzyme reaction.

Substrates are types of enzymes found in the bloodstream.

Substrates are inhibitors that prevent enzyme activity.

Temperature affects enzyme activity by influencing the kinetic energy of molecules. High temperatures may denature enzymes, and low temperatures can slow down reactions.

Temperature has no effect on enzyme activity.

Only high temperatures will enhance enzyme activity.

Enzymes are only active at high temperatures.

Each enzyme has an optimal pH range. Deviations from this range can denature the enzyme or affect its activity and efficiency.

pH levels have no impact on enzyme activity.

Enzymes function best at pH 7.

Enzymes are ineffective in acidic environments.

Enzyme inhibition is the process by which a molecule decreases or stops the activity of an enzyme, either reversibly or irreversibly.

Enzyme inhibition increases enzyme activity.

Enzyme inhibition occurs when enzymes are isolated.

Enzyme inhibition only happens at high temperatures.

Competitive inhibition occurs when an inhibitor competes with the substrate for the active site, while non-competitive inhibition occurs when an inhibitor binds to a site other than the active site, altering enzyme activity.

Competitive inhibition strengthens enzyme activity, while non-competitive weakens it.

Both competitive and non-competitive inhibition occur at the same site on the enzyme.

Non-competitive inhibition is when enzymes self-deactivate.

Enzymes catalyze all metabolic reactions, enabling cells to convert molecules to different products and transfer energy.

Enzymes are not involved in metabolism.

Enzymes slow down metabolic reactions.

Enzymes only participate in digestion-related metabolism.

Cofactors are non-protein chemical compounds that bind to an enzyme and are essential for its activity, often aiding in the catalytic process.

Cofactors permanently deactivate enzymes.

Cofactors are only needed for enzyme production.

Cofactors have no influence on enzyme reactions.

An example is amylase, an enzyme that helps in the digestion of carbohydrates by breaking down starch into sugars.

An example is glucose, an enzyme that supplies energy directly.

Enzymes do not function in digestion.

An example is cholesterol, an enzyme that stabilizes cell membranes.

The lock and key model suggests that the enzyme's active site is a perfect match for the substrate, fitting together precisely like a key in a lock.

The lock and key model indicates enzymes adapt to fit substrates.

The lock and key model refers to enzymes physically storing substrates.

The lock and key model suggests enzymes operate like locks for reacting molecules.

The induced fit model proposes that the active site of the enzyme molds itself around the substrate as it binds, allowing a more snug fit.

The induced fit model states enzymes remain rigid and unchanged during reactions.

The induced fit model is only applicable to synthetic enzymes.

The induced fit model describes enzymes breaking down after reactions.

Yes, enzymes can be reused multiple times as they are not consumed during the reaction they catalyze.

No, enzymes are used up in a single reaction.

Yes, but only if they are heated.

No, enzymes must be replaced after each use.