Enzymes act as catalysts to speed up chemical reactions without being consumed.

Enzymes function as reactants in chemical reactions.

Enzymes are used up in chemical reactions to provide energy.

Enzymes are only involved in breaking down molecules, not building them.

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

It is the area where enzymes are stored in cells.

The active site is where the enzyme’s energy is generated.

The active site is the region that prevents substrate binding.

Enzymes lower the activation energy required for a chemical reaction, making it proceed faster.

Enzymes increase the activation energy needed.

Enzymes do not alter activation energy but increase the reaction rate.

Enzymes eliminate the need for activation energy altogether.

Substrates are the reactants that bind to the enzyme's active site and are transformed into products.

Substrates are products that bind to enzymes.

Substrates are inhibitors of enzymes.

Substrates are created by enzymes to enhance reactions.

Enzyme specificity refers to the ability of an enzyme to choose exact substrates from a group of similar chemical molecules.

Enzyme specificity means one enzyme can act on any substrate.

It indicates how enzymes replicate genetic information.

It shows how enzymes can be interchangeably used in any reaction.

The enzyme-substrate complex forms when an enzyme binds its substrate, allowing the chemical reaction to proceed.

It prevents any chemical reaction from occurring.

It is the final inactive form of an enzyme.

It leads to the destruction of substrates.

Enzyme activity can be affected by factors such as temperature, pH, and substrate concentration.

Only light and humidity affect enzyme activity.

Enzymes are unaffected by external conditions.

Enzyme activity is only affected by electrical charges.

The structure of an enzyme determines its specific function and interaction with substrates.

Enzyme structure is not relevant to its function.

Structure only affects enzyme stability, not function.

Structure has no impact on enzyme efficiency or specificness.

An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity.

It is a molecule that increases enzymes’ productivity.

An inhibitor is a substrate that enhances enzyme binding.

Inhibitors are forms of enzymes with enhanced activities.

Cofactors and coenzymes are non-protein molecules that assist enzymes in catalyzing reactions.

They are proteins that deactivate enzymes.

They are by-products of enzyme reactions with no specific role.

They are always protein-based molecules.

Cofactors can be metals or organic molecules, with coenzymes being a specific type of organic cofactor.

Cofactors are always inorganic ions.

Cofactors are exclusively amino acids.

All cofactors are proteins.

Increasing temperature generally increases enzyme activity, but extreme heat can denature enzymes, reducing activity.

Temperature has no effect on enzyme activity.

Enzyme activity decreases with an increase in temperature.

All enzymes become inactive at higher temperatures.

Each enzyme has an optimal pH range; deviations can alter enzyme shape and function, decreasing activity.

Enzyme activity is not influenced by pH changes.

All enzymes work best in an acidic environment.

Higher pH always enhances enzyme activity.

Competitive inhibition occurs when an inhibitor competes with the substrate for binding to the active site of an enzyme.

It is the enhancement of enzyme activity by substrates.

It occurs when inhibitors activate an enzyme.

The term refers to harmful effects of enzymes at high concentrations.

Enzymes are used in various industries for processes like food preservation, brewing, and cleaning products.

Enzymes are only used in academic laboratories.

They are mostly utilized for genetic modification processes.

Their role is limited to fuel production.