Biochem Flashcards
Catalytic efficiency
Kcat/Km
Km
Substrate concentration at half vmax
Lock and key model
Enzyme specificity
Shape of michaelis menten
Hyperbolic
Competitive inhibition
Inhibitor competes for active site
Increase Km
Uncompetitive inhibition
Inhibitor binds ES
Decrease vmax
Decrease km
Non competitive inhibition
Inhibitor binds E and ES equally
Decrease vmax
Mixed inhibition
Inhibitor binds E and ES unequally
Increase or decrease Km
Decrease vmax
Axes on michaelis menten vs lineweaver burke
V vs (S) 1/V vs 1/(S)
Kcat
Vmax/ [E]
Hills coefficient
If greater than one, indicates cooperative binding
Slope and intercepts lineweaver burke
Slope km/vmax
Y int 1/vmax
Lineweaver for competitive inhibition
No change in y intercept, increasing slopes
Lineweaver for uncompetitive
Same slope increasing y intercept
Lineweaver for non competitive
Increasing slope and y intercept