Environmental Impacts on Enzyme Function - AP Biology

Activation energy. Minimum energy barrier for chemical reactions to proceed.

Multiple polypeptide chains forming a protein. Complex proteins with multiple subunits working together.

Decreases $V_{max}$. Allosteric binding reduces enzyme efficiency.

A site other than the active site for regulation. Regulatory binding site separate from catalytic center.

Activity increases until the enzyme is saturated. More substrate means more enzyme-substrate collisions.

Enzymes have an optimal pH range where they function best. pH changes affect ionization of active site amino acids.

Amino acid sequence. Linear order of amino acids in the protein.

Alpha helices and beta sheets. Regular folding patterns within protein chains.

They reduce activity by altering enzyme shape. Bind elsewhere, changing enzyme conformation.

End product inhibits the pathway. Product accumulation prevents pathway overproduction.

They slow or stop the pathway. Block key enzymes, disrupting metabolic flow.

Holoenzyme. Complete enzyme with all necessary cofactors attached.

Activation energy. Minimum energy barrier for chemical reactions to proceed.

Three-dimensional folding of a polypeptide. Overall 3D shape crucial for enzyme function.

They can inhibit activity by binding to the enzyme. Metals disrupt protein structure and active sites.

Increases $V_{max}$. More enzymes allow higher maximum reaction rates.

Active site changes shape to fit the substrate. Dynamic conformational change upon substrate binding.

Increases until optimal, then decreases. Heat increases motion until denaturation occurs.

Substrate fits exactly into the active site. Rigid complementary shapes for substrate binding.

Denaturation. Loss of secondary and tertiary structure.

The region where substrate molecules bind. Specific shape determines enzyme-substrate interaction.

Results in a lower reaction rate. Fewer substrate molecules limit enzyme-substrate formation.

Multiple polypeptide chains forming a protein. Complex proteins with multiple subunits working together.

Can alter enzyme structure and activity. Changes amino acid sequence, potentially affecting structure.

Coenzymes act as carriers for atoms or functional groups. Organic cofactors that transport chemical groups.

Apoenzyme. Protein component lacking required cofactors for activity.

Increases $K_m$. Higher apparent affinity needed due to competition.

Enzyme activity decreases due to denaturation. Heat breaks bonds maintaining enzyme's 3D structure.

Enzymes catalyze specific reactions. Shape complementarity determines which substrates bind.