Proteins/Enzymes

Question 1

Michaelis-Menten equation

Question 2

What does Km represent in Michaelis-Menten?

Answer 2

affinity of the substrate for the enzyme active site. also represents the substrate concentration needed to achieve half of the maximum reaction rate.

Question 3

lineweaver-burk equation

Question 4

how does a competitive inhibitor impact Vmax and Km?

Answer 4

Does not affect Vmax but increases Km (this is because these inhibitors can be flushed out)

Question 5

how does a non competitive inhibitor affect Vmax and Km?

Answer 5

Does not affect Km but decreases Vmax.

Question 6

how does an uncompetitive inhibitor affect Vmax and Km?

Answer 6

Both Vmax and Km decrease.

Question 7

What does a low Km mean?

Answer 7

High affinity for substrate to active site of enzyme

Question 8

Difference between noncompetitive and uncompetitive inhibition?

Answer 8

In noncompetitive inhibition, the substrate doesn’t need to be bound to the active site for the inhibitor to bind. In uncompetitive inhibition, the binding of the inhibitor actually increases the affinity of the substrate to the active site, decreasing Km.

Question 9

fat-soluble vitamins

Answer 9

A, D, E, and K