Chapter 9: Reaction Mechanisms, Pathways, Bioreactions and Bioreactors


Sketch Non-Competitive Inhibition on a Lineweaver-Burk Plot

Diagram illustrating non-competitive inhibition, showing enzyme (E) binding to substrate (S) to form enzyme-substrate complex (E·S) and converting to product (P). Inhibitor (I) binds to both E and E·S, forming E·I and E·S·I complexes.

\( -r_S = \frac{V_{\max} (S)}{(S) + K_M \left( 1 + \frac{(I)}{K_I} \right) } \)

\( \frac{1}{-r_S} = \frac{(S) + K_M \left( 1 + \frac{(I)}{K_I} \right)}{V_{\max} (S)} \)

\( \frac{1}{-r_S} = \frac{(S) \left( 1 + \frac{(I)}{K_I} \right) + K_M \left( 1 + \frac{(I)}{K_I} \right)}{V_{\max} (S)} \)

\( \frac{1}{-r_S} = \frac{1}{V_{\max}} \left( 1 + \frac{(I)}{K_I} \right) + \frac{K_M}{V_{\max}} \left( 1 + \frac{(I)}{K_I} \right) \frac{1}{(S)} \)

Both slope and intercept change as inhibitor concentration is increased

Lineweaver-Burk plot for noncompetitive enzyme inhibition, showing inverse reaction rate (1/-rs) versus inverse substrate concentration (1/S). The plot includes a 'No Inhibition' line and a set of steeper lines indicating increasing inhibitor (I) concentrations.

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