On the kinetic distinction of ordered and random bireactant enzyme systems

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Abstract

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.

Original languageEnglish
Pages (from-to)914-917
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume68
Issue number3
DOIs
StatePublished - Feb 9 1976

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