It is shown that under certain conditions it could be difficult to distinguish kinetically between an ordered or random addition of two substrates to an enzyme. An ordered mechanism in which substrate binding steps are in rapid equilibrium and which includes the formation of an inactive enzyme-second substrate complex from both directions is indistinguishable by initial velocity, product inhibition, or alternate substrate kinetic studies from a mechanism involving random addition of substrates with ternary complex interconversion as the rate limiting step.
|Number of pages||4|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Feb 9 1976|