Dassinia said:Homework Statement
I have this mixed inhibition, and knowing that it is a thermodynamic cycle i am asked to find the relation between the different Ki and Ks.
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2. Relevant equation
The Attempt at a Solution
I am not even sure to understand the question...
Between E and ES Ks=k-1/k1 Is it equal to k'-1/k'1=Ks' ?epenguin said:
Look at the top line only. What is the equilibrium constant between E and ES?
Well okay since you say you don't understand the question Ks = [E][ S]/[ES] = ?
Now rub out to the arrows of the top line. Leave the others. What is the above-defined equilibrium constant equal to?
Can these equilibrium constants be different?
Dassinia said:Between E and ES Ks=k-1/k1 Is it equal to k'-1/k'1=Ks' ?
Mixed inhibition is a type of enzyme inhibition where the inhibitor binds to both the enzyme and the enzyme-substrate complex. It is important because it affects the rate of the reaction and can give insight into the enzyme's mechanism of action.
Ki, also known as the dissociation constant for the inhibitor, is determined by measuring the reaction rate at different inhibitor concentrations and plotting it on a graph. The x-intercept of this graph is equal to the -Ki value.
Ki and Ks, also known as the dissociation constants for the inhibitor and substrate, respectively, are related by the equation: Ki = Ks(1 + [I]/Ks). This equation shows that Ki is dependent on both Ks and the concentration of the inhibitor.
In competitive inhibition, the inhibitor only binds to the enzyme, while in non-competitive inhibition, the inhibitor can bind to both the enzyme and the enzyme-substrate complex. Mixed inhibition combines elements of both competitive and non-competitive inhibition.
Studying mixed inhibition can provide valuable information about the mechanism of action of enzymes. It can also help in the development of drugs that target specific enzymes and in understanding the effects of different compounds on enzyme activity.