Reading...
Play button
Play button
Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
13 Cards in this Set
- Front
- 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.
|
