3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: (S), mM 0.050 0.075 0.125 0.175 | 0.935 v, (µM min') 0.93 1.264 1.77 2.14 3.7 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW- 10000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
![3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained:
|[S), mM
0.050
0.075
v, (µM min")
0.93
1.264
1.77
2.14
3.7
0.125
0.175
0.935
a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and
Vmax for the enzyme
b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of
final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site
exists per enzyme molecule?
c. Determine the catalytic efficiency for the enzyme
d. The same reactions are performed in presence of an inhibitor A and the resulting
velocities determined:
v plus inhibitor, (µM
min)
0.272
0.37
0.518
0.626
|1.08
|[S), mM
0.050
0.075
0.125
0.175
0.935
Plot these data on the same graph as above and determine the new Km and Vmax and the type
of inhibitor (competitive, non-competitive).
e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb5a1c01f-7615-4a0d-acf4-1e745d51e95a%2Fc5c7ca9b-c36b-4561-b0b1-d134165ef466%2Frskrkd_processed.png&w=3840&q=75)
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