Consider the enzyme-catalyzed conversion of a substrate into a product P in the presence of an inhibitor I with the following properties (mixed inhibition): (i) The inhibitor competes with S to bind the active site of the enzyme with dissoci- ation constant K1 for the complex (EI). (ii) The inhibitor is also capable of binding the enzyme at a secondary site of the enzyme with dissociation constant K{ for the complex (IES). The complex (IES) is unable to form P. iii) The dissociation constants of the (IES) and (EI) complexes satisfy the relation K = K1/2.
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.
![Consider the enzyme-catalyzed conversion of a substrate S into a product
in the
presence of an inhibitor I with the following properties (mixed inhibition):
(i) The inhibitor competes with S to bind the active site of the enzyme with dissoci-
ation constant K¡ for the complex (EI).
(ii) The inhibitor is also capable of binding the enzyme at a secondary site of the
enzyme with dissociation constant K{ for the complex (IES). The complex (IES)
is unable to form P.
iii) The dissociation constants of the (IES) and (EI) complexes satisfy the relation
K{ = K1/2.
What is the value of the ratio vo/(k2 [E]o) when the concentration of the substrate is
[S]o = KM/3 and the concentration of the inhibitor is [I]o = K{/4? Recall that KM is
the Michaelis constant.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0a33fb0f-b96d-4ec9-a130-32f03830082f%2Fb707cd80-9b79-4c86-81ac-5c08507d1afe%2Fy5nr4n_processed.png&w=3840&q=75)
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