Enzymes - AP Biology

Coenzymes. Organic molecules like vitamins that assist in enzyme catalysis.

Isozymes. Different enzyme variants that perform the same catalytic function.

Apoenzyme. The protein part that needs cofactors to become fully functional.

Catalase. Converts toxic $H_2O_2$ into harmless water and oxygen.

Point where increasing substrate does not increase rate. All enzyme active sites are occupied, creating maximum reaction rate.

Saturation. Maximum rate reached when all enzymes are working at full capacity.

Catalase. Converts toxic $H_2O_2$ into harmless water and oxygen.

Isozymes. Different enzyme variants that perform the same catalytic function.

Coenzymes. Organic molecules like vitamins that assist in enzyme catalysis.

Increases activity up to an optimal point; then decreases. Heat increases molecular motion but denatures enzymes at extreme temperatures.

Activity decreases. pH changes alter enzyme shape and charge distribution at the active site.

Inactive enzyme lacking its cofactor. Requires cofactor binding to become catalytically active.

Cofactor. Inorganic helper molecule essential for proper enzyme function.

Increases activity up to an optimal point; then decreases. Heat increases molecular motion but denatures enzymes at extreme temperatures.

Amylase. Breaks down starch into maltose and glucose for energy.

Amino acids. Linked amino acids form the backbone of all enzyme structures.

Lock and key model. Describes how enzyme shape perfectly matches its specific substrate.

Conformation. 3D shape determines function and substrate binding specificity.

Reduces activity regardless of substrate concentration. Binds to allosteric site, changing enzyme shape and reducing function.

Induced fit model. Enzyme slightly changes shape to better accommodate the substrate.

Loss of structure and function. Heat or pH extremes unfold the protein, destroying active site shape.

Site for non-competitive inhibitors or activators. Regulatory binding site separate from the active site.

Activation energy. Energy barrier that enzymes lower to speed up reactions.

Increases rate until substrate saturation. More enzymes mean more active sites until all substrate is bound.

Transition state. High-energy intermediate formed during the enzyme-catalyzed reaction.

NAD+. Essential electron carrier in cellular respiration and metabolism.

Reusable. Enzymes are not consumed and can catalyze multiple reaction cycles.

Inhibitor. Reduces enzyme function through competitive or non-competitive mechanisms.

Active site. This binding region has a specific shape complementary to the substrate.