Environmental Impacts on Enzyme Function - AP Biology
- What is the result of an enzyme being at its optimal pH?
- Maximum activity. Optimal ionization state for catalytic function.
- Identify the effect of a coenzyme on enzyme function.
- Coenzymes act as carriers for atoms or functional groups. Organic cofactors that transport chemical groups.
- What is the tertiary structure of an enzyme?
- Three-dimensional folding of a polypeptide. Overall 3D shape crucial for enzyme function.
- Define the term 'allosteric site' on an enzyme.
- A site other than the active site for regulation. Regulatory binding site separate from catalytic center.
- What is the inactive form of an enzyme without its cofactor?
- Apoenzyme. Protein component lacking required cofactors for activity.
- Identify the primary structure of an enzyme.
- Amino acid sequence. Linear order of amino acids in the protein.
- What is the term for the maximum rate of an enzyme-catalyzed reaction?
- . Achieved when all enzyme active sites are occupied.
- What is an enzyme's active site?
- The region where substrate molecules bind. Specific shape determines enzyme-substrate interaction.
- What is feedback inhibition in enzyme activity?
- End product inhibits the pathway. Product accumulation prevents pathway overproduction.
- What happens to enzyme activity at temperatures above the optimum?
- Enzyme activity decreases due to denaturation. Heat breaks bonds maintaining enzyme's 3D structure.
- Identify the effect of substrate concentration on enzyme activity.
- Activity increases until the enzyme is saturated. More substrate means more enzyme-substrate collisions.
- Identify the term for an enzyme's loss of shape and function.
- Denaturation. Loss of secondary and tertiary structure.
- What is the lock-and-key model of enzyme activity?
- Substrate fits exactly into the active site. Rigid complementary shapes for substrate binding.
- What is the effect of non-competitive inhibition on ?
- Decreases . Allosteric binding reduces enzyme efficiency.
- How does pH affect enzyme activity?
- Enzymes have an optimal pH range where they function best. pH changes affect ionization of active site amino acids.
- What is the effect of enzyme inhibitors on metabolic pathways?
- They slow or stop the pathway. Block key enzymes, disrupting metabolic flow.
- How does extreme pH cause enzyme denaturation?
- It disrupts ionic bonds and hydrogen bonds. Changes in charge distribution destabilize protein structure.
- What is the effect of low temperatures on enzyme activity?
- Decreases activity by slowing molecular motion. Reduced kinetic energy decreases collision frequency.
- What is the secondary structure of enzymes?
- Alpha helices and beta sheets. Regular folding patterns within protein chains.
- What is the effect of a low substrate concentration on enzyme activity?
- Results in a lower reaction rate. Fewer substrate molecules limit enzyme-substrate formation.
- What is the induced fit model of enzyme activity?
- Active site changes shape to fit the substrate. Dynamic conformational change upon substrate binding.
- What is the role of an enzyme in a chemical reaction?
- Lowers activation energy. Stabilizes transition state, making reaction easier.
- What is the active form of an enzyme called?
- Holoenzyme. Complete enzyme with all necessary cofactors attached.
- Describe the effect of non-competitive inhibitors on enzymes.
- They reduce activity by altering enzyme shape. Bind elsewhere, changing enzyme conformation.
- What effect does salinity have on enzyme activity?
- High salinity can denature enzymes. Disrupts water balance and protein stability.
- What is the optimal temperature range for most human enzymes?
- 35°C to 40°C. Body temperature range where enzyme structure remains stable.
- How does competitive inhibition affect ?
- Increases . Higher apparent affinity needed due to competition.
- How does temperature affect the rate of enzyme activity?
- Increases until optimal, then decreases. Heat increases motion until denaturation occurs.
- What is the effect of increasing enzyme concentration on reaction rate?
- Increases reaction rate until substrate is limited. More enzymes provide more active sites for reactions.
- What role do cofactors play in enzyme activity?
- They assist enzymes in catalysis. Inorganic helpers required for proper enzyme function.
- Identify the term for the energy needed to start a reaction.
- Activation energy. Minimum energy barrier for chemical reactions to proceed.
- Identify the impact of heavy metals on enzyme activity.
- They can inhibit activity by binding to the enzyme. Metals disrupt protein structure and active sites.
- What is the effect of a mutation on enzyme function?
- Can alter enzyme structure and activity. Changes amino acid sequence, potentially affecting structure.
- What is the role of vitamins in enzyme activity?
- Vitamins often serve as coenzymes. Essential nutrients converted to active coenzymes.
- How do enzymes increase the speed of reactions?
- By lowering the activation energy. Stabilize transition states to accelerate reactions.
- What is the quaternary structure of enzymes?
- Multiple polypeptide chains forming a protein. Complex proteins with multiple subunits working together.
- Identify the effect of enzyme concentration on .
- Increases . More enzymes allow higher maximum reaction rates.
- What is the result of enzyme saturation?
- Maximum reaction rate is reached. All active sites occupied, no further rate increase.
- What is enzyme specificity?
- Enzymes catalyze specific reactions. Shape complementarity determines which substrates bind.