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chels194 chels194
wrote...
13 years ago
1) For Kinetic experiments performed with increasing cocentrations of an noncompetitive inhibitor, which of the following would be observed?
What Km and Vmax do? decrease or increase

2) Based upon the definition for a competitive inhibitor, which observed kinetic parameters would u anticipate is most affected by the presence of the inhibitor?
Vmax, km and vmax, km, or kcat

3) How do mixed inhibitors effet the apparent Km and Vmax of an enzyme?
Would Km&Vmax decrease, unaffected, increase?

4) About competivtive inhibitors, can  u predict about their presence would affect the apparent Km and Vmax of an enzyme?

Km increase & Vmax same, Km same & Vmax increase, Km decrease& Vmax same, Km and Vmax decrease
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wrote...
Valued Member
Educator
13 years ago
Hey, welcome back chels194!

Here is what I know:

1) Noncompetitive inhibitors (inhibitor binds to enzyme or enzyme+substrate complex): lowers Vmax but Km remains unchanged.

2) Uncompetitive inhibitor binds to Enzyme+substrate complex only! So it lowers Vmax and Km; ratio of Vmax/Km remains unchanged.

3) Mixed inhibitors: Vmax decreases, Km may increase or decreases.

4) Raises Km, Vmax remains unchanged

Bio_man 8)

Enjoy this tutorial Slight Smile

http://www.wiley.com/college/pratt/0471393878/student/animations/enzyme_inhibition/index.html
wrote...
13 years ago
chels if you don't mind me asking, what are you studying and what year is that ? because i don't understand anything in most of your questions  Neutral Face
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