Question

environmental factors affect enzyme reaction rates
reactants, products, and activation energy. underneath the curve, in the box summarize the meaning of the graph.

table columns: environmental factors (high temperature, increasing temperature from cold to warm, lowering temperature, normal temperature, low ph (<6), high ph (>8), neutral ph (6-8), competitive inhibitor, non-competitive inhibitor), affect on enzyme activity (increases (↑), decreases (↓), no change (↔)), denature enzyme? (y/n)

graph: x-axis labeled \energy\ (reversed), y-axis \direction of reaction\, box: \summary of graph:\

Explanation:

To fill the table about how environmental factors affect enzyme reaction rates, we analyze each factor:

1. High Temperature

• Increases Activity?: No (enzyme activity peaks at optimal temp, high temp denatures it).
• Decreases Activity?: Yes (denaturation reduces activity).
• No Change?: No.
• Denature Enzyme?: Y (high temp breaks enzyme’s 3D structure).

2. Increasing Temperature (Cold to Warm)

• Increases Activity?: Yes (up to optimal temp, kinetic energy of molecules increases, more collisions).
• Decreases Activity?: No (before optimal temp, activity rises).
• No Change?: No.
• Denature Enzyme?: N (cold to warm is below denaturation temp).

3. Lowering Temperature

• Increases Activity?: No (lower temp reduces molecular motion, fewer collisions).
• Decreases Activity?: Yes (slower reaction rate).
• No Change?: No.
• Denature Enzyme?: N (low temp slows activity, not denature).

4. Normal Temperature

• Increases Activity?: No (at optimal temp, activity is stable, not increasing further).
• Decreases Activity?: No.
• No Change?: Yes (enzyme works at optimal efficiency).
• Denature Enzyme?: N (normal temp is optimal, no denaturation).

5. Low pH (<6)

• Increases Activity?: No (most enzymes have optimal pH ~7, low pH disrupts structure).
• Decreases Activity?: Yes (acidic conditions reduce activity).
• No Change?: No.
• Denature Enzyme?: Y (extreme pH denatures enzymes).

6. High pH (>8)

• Increases Activity?: No (alkaline conditions disrupt enzyme structure).
• Decreases Activity?: Yes (reduced activity).
• No Change?: No.
• Denature Enzyme?: Y (extreme pH denatures enzymes).

7. Neutral pH (6 - 8)

• Increases Activity?: No (at optimal pH, activity is stable).
• Decreases Activity?: No.
• No Change?: Yes (optimal pH for most enzymes, activity is max and stable).
• Denature Enzyme?: N (neutral pH is optimal, no denaturation).

8. Competitive Inhibitor

• Increases Activity?: No (competes with substrate for active site, reduces effective enzyme - substrate interactions).
• Decreases Activity?: Yes (slows reaction rate).
• No Change?: No.
• Denature Enzyme?: N (binds reversibly to active site, doesn’t denature enzyme).

9. Non - competitive Inhibitor

• Increases Activity?: No (binds to allosteric site, changes enzyme’s shape, reducing activity).
• Decreases Activity?: Yes (reduces enzyme’s catalytic efficiency).
• No Change?: No.
• Denature Enzyme?: N (allosteric binding, not denaturation).

For the energy - reaction graph (assuming it’s a typical enzyme - catalyzed reaction energy profile):

• X - axis: Energy.
• Y - axis: Direction of Reaction (from reactants to products).
• The graph shows that the enzyme - catalyzed reaction has a lower activation energy (the “hump” is smaller) than the uncatalyzed reaction. Reactants have higher energy than products in an exergonic reaction (or vice versa in endergonic, but enzyme - catalyzed reactions often show reduced activation energy). The curve with the enzyme has a lower peak (activation energy) because enzymes lower the activation energy required for the reaction to occur, speeding up the rate of conversion from reactants to products.

Answer:

To fill the table about how environmental factors affect enzyme reaction rates, we analyze each factor:

1. High Temperature

• Increases Activity?: No (enzyme activity peaks at optimal temp, high temp denatures it).
• Decreases Activity?: Yes (denaturation reduces activity).
• No Change?: No.
• Denature Enzyme?: Y (high temp breaks enzyme’s 3D structure).

2. Increasing Temperature (Cold to Warm)

• Increases Activity?: Yes (up to optimal temp, kinetic energy of molecules increases, more collisions).
• Decreases Activity?: No (before optimal temp, activity rises).
• No Change?: No.
• Denature Enzyme?: N (cold to warm is below denaturation temp).

3. Lowering Temperature

• Increases Activity?: No (lower temp reduces molecular motion, fewer collisions).
• Decreases Activity?: Yes (slower reaction rate).
• No Change?: No.
• Denature Enzyme?: N (low temp slows activity, not denature).

4. Normal Temperature

• Increases Activity?: No (at optimal temp, activity is stable, not increasing further).
• Decreases Activity?: No.
• No Change?: Yes (enzyme works at optimal efficiency).
• Denature Enzyme?: N (normal temp is optimal, no denaturation).

5. Low pH (<6)

• Increases Activity?: No (most enzymes have optimal pH ~7, low pH disrupts structure).
• Decreases Activity?: Yes (acidic conditions reduce activity).
• No Change?: No.
• Denature Enzyme?: Y (extreme pH denatures enzymes).

6. High pH (>8)

• Increases Activity?: No (alkaline conditions disrupt enzyme structure).
• Decreases Activity?: Yes (reduced activity).
• No Change?: No.
• Denature Enzyme?: Y (extreme pH denatures enzymes).

7. Neutral pH (6 - 8)

• Increases Activity?: No (at optimal pH, activity is stable).
• Decreases Activity?: No.
• No Change?: Yes (optimal pH for most enzymes, activity is max and stable).
• Denature Enzyme?: N (neutral pH is optimal, no denaturation).

8. Competitive Inhibitor

• Increases Activity?: No (competes with substrate for active site, reduces effective enzyme - substrate interactions).
• Decreases Activity?: Yes (slows reaction rate).
• No Change?: No.
• Denature Enzyme?: N (binds reversibly to active site, doesn’t denature enzyme).

9. Non - competitive Inhibitor

• Increases Activity?: No (binds to allosteric site, changes enzyme’s shape, reducing activity).
• Decreases Activity?: Yes (reduces enzyme’s catalytic efficiency).
• No Change?: No.
• Denature Enzyme?: N (allosteric binding, not denaturation).

For the energy - reaction graph (assuming it’s a typical enzyme - catalyzed reaction energy profile):

• X - axis: Energy.
• Y - axis: Direction of Reaction (from reactants to products).
• The graph shows that the enzyme - catalyzed reaction has a lower activation energy (the “hump” is smaller) than the uncatalyzed reaction. Reactants have higher energy than products in an exergonic reaction (or vice versa in endergonic, but enzyme - catalyzed reactions often show reduced activation energy). The curve with the enzyme has a lower peak (activation energy) because enzymes lower the activation energy required for the reaction to occur, speeding up the rate of conversion from reactants to products.