Why is Km considered an intrinsic property of an enzyme?

Given the rate constants k1 = 2 M^-1s^-1, k-1 = 1 s^-1, and k2 = 0.5 s^-1, calculate the Km for the enzyme under steady state conditions.

If enzyme A has a Km of 0.1 M and enzyme B has a Km of 0.5 M, which enzyme has a stronger affinity for its substrate?

Which of the following expressions correctly represents Km in terms of rate constants?

Why does Km remain constant despite changes in enzyme concentration?

Why is the ratio (k-1 + k2) / k1 used to calculate Km?

How can you verify that Km has units of molarity using rate constants?