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Unformatted text preview: 1 Inhibition Studies • Important Structural Moieties of Substrates • Enzyme Regulation in the Cell • Drug Studies • Effects on k cat & K m • Solve for K I by comparing Km values. • Km’/Km = alpha • Km’ = apparent Km due to presence of inhibitor • Note: Km does not change • Alpha = 1 + [I] o /K I (more on this after qz 4) Competitive Inhibitor • Inhibitor lowers the rate of formation of the ES complex. – Rate = k 1 [E][S] – No change in k 1. – Change in [E] = or Apparent [E] = [E] + [EI] – But when [S] = ∞ , Inhibitor cannot outcompete. Thus, Vmax = same as no inhibitor set. • Why is the apparent Km increasing? – Recall Km = Rate breakdown/Rate of formation. – Rate of formation Inhibition Studies: Alpha • Alpha – For competitive inhibitors: the factor by which the inhibitor reduces binding af¡nity. – α = 2, then you need twice the substrate to obtain velocity of the “no inhibitor” reaction....
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This note was uploaded on 10/07/2010 for the course POLI SCI 40 taught by Professor Sch during the Spring '10 term at UCLA.
- Spring '10
- American Politics