Question

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

Science   Chemistry   
0 0
Add a commentTranscribed image text
Next >

Homework Answers

Answer #1

a)They decrease the apparent KM - False

Ans: The apparent Km increases in competitive inhibition.

(b) They decrease Vmax - false

Ans: Vmax has no effect in competitive inhibition

(c) They increase KM / Vmax - false

Ans: In the presence competitive inhibitor Km increase but Vmax is unaffected.

(d) Inhibition cannot be overcome by adding more [S] - False

Ans: By adding more substrate inhibition can over come

(e) They bind to a different site from the substrate- False

Ans: Inhibitor binds to the same site where substrate binds

0 0
Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Log In

Sign Up

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
1. Which of these is true of competitive enzyme inhibitors? Select all correct answers. A. Competitive...
1. Which of these is true of competitive enzyme inhibitors? Select all correct answers. A. Competitive inhibitors lower the enzyme's kcat B. Competitive inhibitors often resemble the substrate C. Competitive inhibitors bind at the same site as the enzyme's substrate D. Competitive inhibitors permanently inhibit the enzyme, even after removal E. Competitive inhibitors effectively raise the enzyme's Km 2. An antibody-antigen pair is found to bind with a Kd of 25 nM. Replacing three Phe at the binding site with...
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...
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 statement is TRUE about enzyme inhibition? A. In competitive inhibition the inhibitor binds to the...
Which statement is TRUE about enzyme inhibition? A. In competitive inhibition the inhibitor binds to the allosteric site of the enzyme B. In competitive inhibition the inhibitor binds to the active site of the enzyme C. In irreversible inhibition, a poison binds to the enzyme so that it can neverwork D. All above are true
Which of the followings are true about the active site of an enzyme? A. It binds...
Which of the followings are true about the active site of an enzyme? A. It binds the substrate B. It is the regulation site of the enzyme C. Inhibitor binds active sites under competitive inhibition D. The energy released by active site-substrate binding can lower the activation energy It has multiple answers
Which of the followings are true about the active site of an enzyme? A. It binds...
Which of the followings are true about the active site of an enzyme? A. It binds the substrate B. It is the regulation site of the enzyme C. Inhibitor binds active sites under competitive inhibition D. The energy released by active site-substrate binding can lower the activation energy It has multiple answers
If an enzyme reaction rate is approaching the Vmax, with a large excess of substrate present,...
If an enzyme reaction rate is approaching the Vmax, with a large excess of substrate present, which of the following would have the least effect on the rate of reaction? Add moderate amount of a competitive inhibitor Add a moderate amount of a non-competitive inhibitor Add more enzyme to the mixture Add a moderate amount of an irreversible inhibitor Decrease the Temperature of the Reaction by a moderate amount How can Vmax be approached despite the presence of a competitive...
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
indicate whether each of the following statements about allosteric enzymes is true or false: A) they...
indicate whether each of the following statements about allosteric enzymes is true or false: A) they always have quaternary protein structure B) They have two regulatory sites C) regulators can decrease but not increase enzyme activity d) both substrate and regulator often bind at the same site
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.
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT