Lecture 13- Kinetics Flashcards
Km
Michaelis constant; [S] where rxn rate is half maximal OR half of the active sites are full
vmax
Maximum velocity; Maximum rate possible for a given concentration of enzyme
Kcat
Turnover number; Number of substrate molecules converted per active site per time (first order rate constant)
Ks
A dissociation constant for substrate binding
Kcat/Km
Specificity constant; Measure of enzyme performance by predicting the fate of ES
-1/Km
x-intercept
1/vmax
y-intercept
Reversible inhibitors
- Competitive
- Non-competitive (allosteric)
- Uncompetitive (allosteric)
Competitive inhibition
vmax is constant
Km is a variable
Non-competitive inhibition
vmax is variable
Km is constant
Uncompetitive inhibition
vmax is variable
Km is variable
Irreversible inhibitors (inactive enzymes)
- Group-specific
- Substrate analogs
- Suicide inhibitors
Group-specific
- Targets a specific AA
- Specificity for active site: Low
Substrate analogs
- Substrate mimic, modifies enzyme
- Specificity for active site: High
Suicide inhibitors
- Modified substrate so is unable to form products
- Specificity for active site: Very high