16 01 Oct 2010

16 01 Oct 2010 - Inhibitors Irreversible inhibition...

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Inhibitors Irreversible inhibition – modification eliminates activity Reversible inhibition – the inhibitor is in equilibrium (can bind and come off) 1. Competitive inhibition – compete with substrate for the active site ( [E], [EI], and [ES]) 2. Uncompetitive inhibition – bind to allosteric site in the presence of substrate ([E], [ES], and [ESI]) 3. Mixed inhibition – bind either E or ES ([E], [ES], [EI], and [ESI]) Modify the M-M to include inhibition α K + [S] E + I EI K I = [E][I] / [EI] [EI]/[E] = [I]/K I α = 1 + [I]/K I
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Competitive inhibition - increasing [I] increases the apparent Km (lower affinity) - more [S] is required to reach Vmax / 2 Vmax (y intercept) is not affected α in the x intercept denominator
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Uncompetitive inhibition (allosteric) - increasing [I] decreases the apparent Km (higher affinity) - i.e. less free [E] Vmax decreases as [I] increases α in the x intercept numerator
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Mixed inhibition (allosteric and independent of substrate) Increasing [I] increases the apparent Km Vmax decreases as [I] increases α in the x intercept numerator and denominator
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This note was uploaded on 09/18/2011 for the course CHEM 3510 taught by Professor Mueser during the Spring '10 term at Toledo.

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16 01 Oct 2010 - Inhibitors Irreversible inhibition...

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