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    The following graph represents the enzyme kinetics observed for an enzyme (E) in the presence of two different inhibitors, P and Q, each at two differ
    Question


    The following graph represents the enzyme kinetics observed for an enzyme (E) in the presence of two different inhibitors, P and Q, each at two different concentrations (x-axis: −1/v; y-axis: −1/[S]).

    Based on the graph, what is the substrate concentration (in μM) at which both inhibitors achieve 50% inhibition?

    A.

    0.333

    B.

    0.5

    C.

    1.0

    D.

    2.0

    Correct option is C


    Correct Answer:
    (c) 1.0 μM
    Explanation:
    Fifty percent inhibition corresponds to a condition where the reaction velocity is half of the uninhibited velocity at the same substrate concentration.
    On a Lineweaver–Burk plot, this is identified by comparing inhibitor lines with the control line at a common 1/[S] value where the increase in 1/v reflects 50% loss of activity.
    From the graph, both inhibitors P and Q show their 50% inhibitory effect at 1/[S] = 1, corresponding to [S] = 1.0 μM.
    Information Booster :
    · Lineweaver–Burk plots help visualize inhibitor effects on Km and Vmax.
    · A 50% reduction in velocity is a standard reference point for comparing inhibitor strength.
    · Identical inhibition at a given [S] implies comparable functional inhibition under those conditions.
    · Reciprocal plots allow easy substrate concentration estimation from straight-line intersections.
    Additional Information (Incorrect Options):
    0.333 μM and 0.5 μM: These correspond to higher 1/[S] values where inhibition differs between P and Q.
    2.0 μM: At higher substrate concentrations, inhibition is less pronounced and does not reflect 50% inhibition for both inhibitors simultaneously.

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