What is the inhibition constant (KI) in the context of enzyme-inhibitor interactions?

How does the inhibition constant for the free enzyme (KI) differ from the inhibition constant for the enzyme-substrate complex (K'I)?

How can the inhibition constant (KI) be derived similarly to the Michaelis constant (KM) by substituting substrate concentration with inhibitor concentration?

Given the inhibition constants KI = 0.1 M and K'I = 0.5 M, which complex has a higher affinity for the inhibitor?

How can the inhibition constant for the free enzyme (KI) and the enzyme-substrate complex (K'I) be used to determine the preferred binding site of an inhibitor?

If the dissociation rate constant (k-EI) is 1.0 s^-1 and the association rate constant (kEI) is 5.0 M^-1s^-1, what is the inhibition constant (KI)?

Given KI = 0.2 M and KM = 0.5 M, which constant indicates a stronger binding affinity?