BCH 351: EXAM 2 REVIEW UPDATED ACTUAL
QUESTIONS AND CORRECT ANSWERS
Question:
1. A substance that increases reaction rate by lowering activation energy without
being permanently changed.
Answer:
Catalyst
Question:
2. Activation Energy (Ea)
Answer:
The energy barrier that reactants must overcome to reach the transition state.
Question:
3. Entropic Factor in Catalysis
Answer:
Catalyst aligns and brings reactants into close proximity to easily form the
transition state.
Question:
4. Enthalpic Factor in Catalysis
Answer:
Strong binding of reactants to the catalyst in the transition state.
Question:
5. Proximity Effect
Answer:
Positioning substrates close together, enhancing reaction rates by a factor of
about 5.
, Question:
6. Orientation Effect
Answer:
Aligning substrates properly relative to each other, increasing reaction rates up to
100-fold.
Question:
7. Induced-Fit Model
Answer:
Weak initial substrate binding induces conformational changes in the enzyme to
strengthen binding.
Question:
8. Uniform vs. Differential Binding
Answer:
Uniform increases both substrate and transition state affinity; differential increases
only transition state affinity.
Question:
9. Michaelis-Menten Equation
Answer:
v = (Vmax * [S]) / (Km + [S])
Question:
10. Michaelis Constant (Km)
Answer:
The substrate concentration at which the reaction rate is at half-maximum
(Vmax/2).
Question:
11. Turnover Number (kcat)
Answer:
The maximum number of substrate molecules converted to product per enzyme
active site per second.
QUESTIONS AND CORRECT ANSWERS
Question:
1. A substance that increases reaction rate by lowering activation energy without
being permanently changed.
Answer:
Catalyst
Question:
2. Activation Energy (Ea)
Answer:
The energy barrier that reactants must overcome to reach the transition state.
Question:
3. Entropic Factor in Catalysis
Answer:
Catalyst aligns and brings reactants into close proximity to easily form the
transition state.
Question:
4. Enthalpic Factor in Catalysis
Answer:
Strong binding of reactants to the catalyst in the transition state.
Question:
5. Proximity Effect
Answer:
Positioning substrates close together, enhancing reaction rates by a factor of
about 5.
, Question:
6. Orientation Effect
Answer:
Aligning substrates properly relative to each other, increasing reaction rates up to
100-fold.
Question:
7. Induced-Fit Model
Answer:
Weak initial substrate binding induces conformational changes in the enzyme to
strengthen binding.
Question:
8. Uniform vs. Differential Binding
Answer:
Uniform increases both substrate and transition state affinity; differential increases
only transition state affinity.
Question:
9. Michaelis-Menten Equation
Answer:
v = (Vmax * [S]) / (Km + [S])
Question:
10. Michaelis Constant (Km)
Answer:
The substrate concentration at which the reaction rate is at half-maximum
(Vmax/2).
Question:
11. Turnover Number (kcat)
Answer:
The maximum number of substrate molecules converted to product per enzyme
active site per second.