For enzymes that follow Michaelis–Menten kinetics, the
inhibitors that inhibit enzyme activity include reversible
inhibitor and irreversible inhibitor.
1. Describe the type of reversible inhibitor.
2. Suggest ways to distinguish between types of inhibitors through
enzyme reaction experiments.
What is competitive and uncompetitive reversible inhibition? And
how are they similar? and most importantly, how is their effect on
rate at which is can transform a substrate different?
Using the
Michaelis-Menten equation, derive an expression that will
determine Km
as a function or in
terms of Vmax,
V0
and [S]. With this
derived equation then calculate:
a)
Km
B) Indicate at
each substrate concnetration whether this Km changes with the
changing S
C)
Using the double
reciprocal plot, determine Km.
What are the key differences between the Michaelis-Menten model
that describes enzyme kinetics and the Monod model that describes
whole-cell or community kinetics?
Draw a Michaelis Menten graph to represent normal pyruvate
carboxylase kinetics in the conversion of pyruvate to oxaloacetate.
Explain why you drew things as you did.
Initial rate data for an enzyme that obeys Michaelis-Menten
kinetics are shown in the following table. When the enzyme
concentration is 3 nmol ml−1, a Lineweaver-Burk plot of this data
gives a line with a y-intercept of 0.00426
(μmol−1ml s).
[S] μM
v0 (μmol ml−1 s−1)
320
169
160
132
80.0
92.0
40.0
57.2
20.0
32.6
10.0
17.5
a. Calculate Kcat for the reaction
b. Calculate Km for the enzyme
cWhen the reactions in part (B) are repeated in the...