columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 Им. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme a. C. e. [S] (mM) (1) V. {(umol/(ml.s)] (2) V. [[umol/(ml.s)]| 4.4 (3) V. umol/{ml.s] 6.6 11.4 76 14.6 8.6 26.6 16.4 29 8 17.8 24.6 28.2 16 45.8 24 60 40.8
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.
![columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
Им.
Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and Ky for the enzyme
a.
C.
e.
[S] (mM)
(1) V.
{(umol/(ml.s)]
(2) V.
[[umol/(ml.s)]|
4.4
(3) V.
umol/{ml.s]
6.6
11.4
76
14.6
8.6
26.6
16.4
29 8
17.8
24.6
28.2
16
45.8
24
60
40.8](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F70652d85-66a2-4434-9ba6-c6db24aab6c1%2F409dbe72-5f08-4327-841a-3ad904fd57fe%2Fqela44d.jpeg&w=3840&q=75)
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