(a) Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe how ATP interacts with the enzyme in the case of no AMP (•). (b) Explain the physical significance of the displacement of the Hill plots to the right in panel B with respect to the binding of AMP and ATP to the allosteric effector sites on 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.
![2. The two diagrams to the right il-
lustrate plots of steady-state ki-
5FA
0.8
netic studies to characterize the in-
nH =
3.5
0.6-
teraction of heart muscle phos-
phofructokinase-1 with a non-phy-
siological, synthetic substrate fruc-
tose-6-sulfate. Because the kcat is
0.4-
0.2-
smaller than that for the natural
10 μΜ
20 μΜ
48 μΜ
substrate, higher enzyme concen-
trations could be used. The results
show the influence of increasing
0.2
0.4
concentrations of ATP on the initial
-0.6-
>
velocity of the enzyme catalyzed
reaction in the presence of no
-0.8
4
12
20
28
36
44
52
60
68
76
84
92
1.2
2.0
2.4
AMP (•), 10 µM AMP (•), 20 µM
AMP (-), and 48 µM AMP ().
[ΑΤPΙ (μM)
log[ATP] (µM)
(а)
how ATP interacts with the enzyme in the case of no AMP (•).
Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe
(b)
with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme.
Explain the physical significance of the displacement of the Hill plots to the right in panel B
10 (umoles/min/mg)
log (Vm
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