BCH 361 Lecture Notes - Lecture 2: Specific Activity, Dissociation Constant
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1. A) Activity refers to the amount of enzyme transformed in a specific number of unit time. In my
answer, I used micromoles per minute.
a. 12 millimoles -> 12000 μm.
b. Activity = enzyme transformed / unit time = (12000 μm) / (2 min) = 6000 μm/min
c. B) Specific activity refers to the units of activity per mg
d. Specific activity = activity / total mg of enzyme = (6000 μm/min) / (24 mg) = 250
2. At substrate concentrations, near the Km, the enzyme displays significant catalysis yet is
sensitive to changes in substrate concentration.
3. The sequential reactions are characterized by the formation of a ternary complex
consisting of the enzyme & both substrates. Double-displacement reactions always
require the formation of a ternary complex consisting of the enzyme and both substrates.
Double-displacement reactions always require the formation of a temporary substituted
4. Km is the Michaelis-Menten constant which represents the concentration of the
substrate when the rate of reaction is equal to '1/2' of the maximum velocity for the
reaction. It can also be thought of as a measure of how well a substrate complexes
with a given enzyme, otherwise in common it is known as its binding affinity.
a. And as mentioned above when
b. Rate of reaction = ( Rate )max/2
c. Then Km = Kd
5. A.Rate = [S t2] - [S t1] / t2-t1 = mol/min
Initial concentration (μmol/mL)
Initial Rate (mol/min)