*OBJ - Enzyme Kinetics

Question 1

Define rate constant of a ligand protein interaction, and correlate rate constants toKaandKd

Answer 1

a

Question 2

Describe how measurable parameters can be used to determine the initial velocity of an enzyme catalyzed reaction using the Michaelis-Menten equation

Answer 2

a

Question 3

DefineKm, and describe its practical implication in understanding the efficiency of an enzyme-catalyzed reaction

Answer 3

a

Question 4

Deduce the Michaelis-Menten equation from the ligand-binding equation

Answer 4

a

Question 5

Distinguish between ligand binding and enzyme catalysis, and describe the relationship betweenKmandKd

Answer 5

a

Question 6

DefineVmax, and explain what is meant by saturation kinetics

Answer 6

a

Question 7

Explain the mechanistic significance of the hyperbolic nature of the Michaelis-Menten curve

Answer 7

a

Question 8

Define isozymes, and explain the physiological significance of different isoforms having differentKms for substrate

Answer 8

a

Question 9

Explain what is meant by reversible inhibition of enzymes, and describe the mechanistic difference between reversible and irreversible inhibitions

Answer 9

a

Question 10

Explain the Lineweaver-Burke (double reciprocal) transformation of the Michaelis-Menten equation

Answer 10

a

Question 11

Distinguish between competitive, noncompetitive and uncompetitive reversible inhibition, and demonstrate how the double reciprocal plot can be used to discriminate one mechanism from the other

Answer 11

a