Question

1.   Which of the following is true of enzyme catalyzed reactions? a.   Reaction rates are temperature dependent b.   Reaction...

1.   Which of the following is true of enzyme catalyzed reactions?

a.   Reaction rates are temperature dependent

b.   Reaction rates are pH dependent

c.   Reaction rates depend on substrate concentration

d.   Reaction rates depend on enzyme structure

e.   All of the above

f.    a, b, and c

2.   Which of the following is NOT true of enzymes?

a.   Enzyme activity depends on reaction conditions.

b.   Enzymes are catalysts that decrease the rate of reaction.

c.   Enzymes can be inhibited by other proteins

d.   Enzymes do not alter the change in free energy (ΔG) of the reaction.

3.   For a given reaction involving an enzyme, competitive inhibitors will cause Vmax to (increase/decrease/stay the same), while causing Km to (increase/decrease/stay the same).

4.   Below the optimal temperature, increasing the temperature of an enzyme-catalyzed reaction will (increase/decrease/not change) its reaction rate, whereas above the optimal temperature, an increase in temperature will (increase/decrease/not change) the reaction rate.

Homework Answers

Answer #1

1. Answer: Option E is correct
Explanation:
Reatction rate of an enzyme catalyzed reaction is dependent on several factors
i. Temperature
ii. pH
iii. Substrate concnetration
iv. Presence of activators or inhibitors that alter the enzyme structure and its affinity for the substrate

2. Answer: Option B is correct
Explanation:
Enzymes are biocatalysts that increase the rate of reactions by multiple mechanisms
i. By decreasing the activation energy
ii. By increasing the effective concnetrations of substrates

3. A competitive inhibitor resembles the structure of the substrate and competes for the same active site on the enzyme
It increases the Km but does not affect Vmax.

4. Any deviation (increase or decrease) in temperature from the optimal range decreases the reaction rate.

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
The zero order rate is seen in an enzyme catalyzed reaction when: A. There is too...
The zero order rate is seen in an enzyme catalyzed reaction when: A. There is too much enzyme and too little substrate B. Enzyme reactions are always first order C. The Michaelis constant is very high D. The Vmax of the reaction is twice that which is observed E. The enzyme substrate comples is at its maximum concentration What happens when you add more enzyme to a catalyzed reaction that already is proceeding at Vmax? A. The reaction is inhibited...
Which of the following statement concerning enzyme-catalyzed reactions is CORRECT? The rate of an enzyme catalyzed...
Which of the following statement concerning enzyme-catalyzed reactions is CORRECT? The rate of an enzyme catalyzed reaction is independent of substrate concentration. At saturating levels of substrate, the rate of an enzyme –catalyzed reaction is proportional to the enzyme concentration. The Km for a regulatory enzyme varies with enzyme concentration. If enough substrate is added, the normal Vmax of an enzyme –catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. The sigmoidal shape of the v-versus...
16. Which of the following is NOT true about enzymes? A) Some enzymes require cofactors. B)...
16. Which of the following is NOT true about enzymes? A) Some enzymes require cofactors. B) Enzyme inhibitors may interact either reversibly or irreversibly with an enzyme to alter its Km and /or Vmax values. C) Transition state stabilization can significantly increase the activation energy for a reaction. D) Enzymes typically act under milder conditions of temperature and pH than (nonenzyme) chemical catalysts. E) Zymogens are a form of inactive precursors of enzyme.
Which of the following statements about competitive inhibitors of an enzyme reaction is true? (a) They...
Which of the following statements about competitive inhibitors of an enzyme reaction is true? (a) They decrease the apparent KM (b) They decrease Vmax (c) They increase KM / Vmax (d) Inhibition cannot be overcome by adding more [S] (e) They bind to a different site from the substrate
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B)...
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B) Vmax (maximum velocity) C) kcat (turnover number) D) A and B E) B and C Km is the equivalent of: A) Substrate concentration at Vo B) Substrate concentration when Vmax is reached C) Substrate concentration when 1/2 Vmax is reached D) Product concentration when 1/2 Vmax is reached
Enzymes are true catalysts because A. they decrease the energy of activation required for the reactions...
Enzymes are true catalysts because A. they decrease the energy of activation required for the reactions they participate in. B. they are required in small amounts and are not consumed in the reaction. C. they increase reaction rates without altering the chemical equilibrium between reactants and products D. All of the above 26. Estimate, by inspection (i.e., no need to use a graph), of the Vmax and Km of an enzyme-catalyzed reaction for which the following data were obtained (pay...
1. true or false: substrates frequently bind to the active site of enzymes using a covalent...
1. true or false: substrates frequently bind to the active site of enzymes using a covalent bond 2. true or false: a competitive inhibitor of an enzyme-catalyzed reaction maintains the same Vmax of the reaction and increase the KM 3. when dividing cells, the physical separation of chromosomes during the mitotic phase depends on what molecular complexes? a. microtubules b. myosin and actin filaments c. myosin d. kinesin e. microtubules motors and microtubule
Questions about biochem: 1.) If the ΔG'° of the reaction A --> B is +1000 kJ/mol,...
Questions about biochem: 1.) If the ΔG'° of the reaction A --> B is +1000 kJ/mol, under standard conditions the reaction will never reach equilibrium. True or False ? 2.) An enzyme catalyzes the reaction A↔B. The enzyme is present at a concentration of 4 nm, and the Vmax is 1.5 µM s-1. The Km for substrate A is 10 µM. Which of the following is the initial velocity of the reaction Vo when the substrate concentration is 10 µM?...
QUESTION 1 Which of the following does NOT apply to an enzyme? A. Catalyst B. Inorganic...
QUESTION 1 Which of the following does NOT apply to an enzyme? A. Catalyst B. Inorganic C. Protein D. All apply to an enzyme QUESTION 2 When an enzyme catalyzes a reaction: A. Substrate(s) bind in the active site B. Products bind in the active site C. The shape of the enzyme remains unchanged D. The enzyme is consumed by the reaction QUESTION 3 Which of the following would interfere most with the ability of an enzyme to catalyze a...
In an enzyme-catalyzed reaction, which of the following events occurs in the transition state facilitation stage?...
In an enzyme-catalyzed reaction, which of the following events occurs in the transition state facilitation stage? a. The enzyme allows substrates interact, increasing the activation energy of the reaction b. Substrates, cofactors, and coenzymes undergo initial binding to the active site of the enzyme c. The enzyme allows substrates to interact, lowering the activation energy of the reaction d. The products are released from the enzyme e. The enzyme allows substrates to interact, lowering the Gibbs free-energy change of the...