Uni Uni Reaction with Non-Competitive Partial Inhibition (Q6684692): Difference between revisions

Enzyme (E) and Substrate (S) form an enzyme-substrate complex (ES), which catalyzes the formation of product (P). Rates for complex formation and dissociation are $k_{1}$ and $k_{-1}$, $k_{2}$ is the rate of the rate-determining enzymatic step of product formation. Free enzyme and the enzyme-substrate complex may bind an inhibitor (I) to form an enzyme-inhibitor (EI) and enzyme-inhibitor-substrate complex (EIS) with $k_{3}$ or $k_{-3}$ and $k_{4}$ or $k_{-4} as rates of inhibitor complex formation and depletion. Enzyme-inhibitor complex and enzyme-inhibitor-substrate convert into each other with rates $k_{5}$ and $k_{-5}$. In the non-competitive case: $k_{3} = k_{4}$, $k_{-3} = k_{-4}$, $k_{5} = k_{1}$ and $k_{-5} = k_{-1}$. The enzyme-inhibitor-substrate complex can form product with rate $k_{6}.