Uni Uni Reaction with Competitive Partial Inhibition (Q6684687): Difference between revisions

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Changed claim: description (P1459): 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 inhibit...
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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 $k_{-5}$. From the enzyme-inhibitor-substrate complex product is formed with rate $k_{2}$. Properly this is a mixed partial inhibition in which the inhibitor does not affect the turnover rate,
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. From the enzyme-inhibitor-substrate complex product is formed with rate k₂. Properly this is a mixed partial inhibition in which the inhibitor does not affect the turnover rate.

Revision as of 10:20, 9 May 2025

uni uni reaction with inhibition
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Uni Uni Reaction with Competitive Partial Inhibition
uni uni reaction with inhibition

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    Q6032837 (Deleted Item)
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    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. From the enzyme-inhibitor-substrate complex product is formed with rate k₂. Properly this is a mixed partial inhibition in which the inhibitor does not affect the turnover rate.
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