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13 Cards in this Set
- Front
- Back
What is K_m?
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The Michaelis constant:
K_m= (k1+k2)/k1 K_m= 1/2 v_max Where k1= rxn rate constant of E+S<--> ES k2= rxn rate constant of ES->E+P |
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The Michaelis-Menten Equation
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v=(v_max*[S])/K_m +[S]
Where S= substrate; v= velocity |
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What is the Steady State Assumption?
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The assumption that [ES] quickly reaches a constant value in a dynamic system of the rxn.
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What is a turnover number, molecular/ enzymatic activity?
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k_cat: the maximum number of substrate molecules converted to product per enzyme molecule per unit of time.
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What is One International Unit
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The amount of enzyme that catalyzes the formation of 1 micromole of Product in 1 minute.
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What is Specific Activity (SA)?
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the amount of enzyme needed to convert
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What are the 3 main types of Reversible Inhibition?
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Competitive, Mixed Non-competitive, and Uncompetitive
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What is Competitive Inhibition?
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The binding of an inhibitor to the enzyme's active site.
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Describe the relationship between K_m and v_max in Competitive Inhibition.
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V_max remains the same for concentrations with or without inhibitor, however K_m changes.
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What is Mixed Non-competitive Inhibition?
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The binding of an inhibitor to the a site other than the active site of an enzyme or the ES complex. This may result in a conformational change which affect substrate binding/conversion to product.
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Describe the relationship between K_m and v_max in Non-competitive Inhibition.
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V_max & K_m both change randomly.
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What is Uncompetitive Inhibition?
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The binding of an inhibitor to the ES complex only.
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Describe the relationship of K_m and v_max in the Lineweaver-Burke Plot.
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K_m & v_max are both different, but parallel. Both lines are parallel.
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