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13 Cards in this Set

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  • Back
What is K_m?
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
The Michaelis-Menten Equation
v=(v_max*[S])/K_m +[S]

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