uni uni reaction with non-competitive complete inhibition
| research problem |
Available identifiers
uni uni reaction with inhibition
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 k₁ and k₋₁, k₂ 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 k₃ or k₋₃ and k₄ or k₋₄ as rates of inhibitor complex formation and depletion. Enzyme-inhibitor complex and enzyme-inhibitor-substrate convert into each other with rates k₅ and k₋₅. In the non-competitive case: k₃ = k₄, k₋₃ = k₋₄, k₅ = k₁, and k₋₅ = k₋₁. The enzyme-inhibitor-substrate complex cannot form product, the inhibition is thus complete.
Research problems specializing uni uni reaction with non-competitive complete inhibition
| initial reaction rate of uni uni reaction without product and non-competitive complete inhibition |
Further items linking to uni uni reaction with non-competitive complete inhibition
| Item | Property |
|---|---|
| enzyme kinetics | contains |
| uni uni reaction with reversible complete inhibition | specialized by |
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