BIO Exam 2: Enzymes (2) Flashcards
(9 cards)
Enzymology
Enzymes lower activation energy to increase rate.
No effect on DGo’ or Keq
Vmax reflects catalysis rate
Km reflects substrate binding
Specific Activity
Comparing enzymes: Grow cultures, lyse cells, measure vi
Usually, compare the specific activity
Normalize to the total amount of protein present
Controlling Enzyme Activity
Many enzymes can be regulated by a post-translational modification
Competitive Inhibition
Many enzymes can be regulated by a other small molecules
Competitive Inhibitors bind to the active site
No catalysis
Compete with the substrate for binding
No effect on Vmax
Km is increased
Noncompetitive Inhibitors
Not all inhibitors bind the active site
Some bind to an allosteric site. Binding changes enzyme conformation.
Noncompetitive (or allosteric) inhibitors
How will an allosteric inhibitor affect Vmax and Km?
Two subclasses:
Pure noncompetitive inhibitors
Lowers Vmax; No effect on Km
Mixed noncompetitive inhibitors
Lowers Vmax; Raises Km
Enzyme Activators
Some small molecules do the opposite: activators
Always allosteric
May be pure (raises Vmax, no effect on Km)or mixed (raises Vmax, lowers Km
Enzymes and pH: How would the pH affect the an enzyme’s function?
Non-ideal pH denatures some of the enzymes
each enzyme has its own optimal pH
Each enzyme has a different optimum
Hess’ Law
Enzymes can’t change a DGo’ but can help overcome it
Energetic coupling of two reactions together. Hess’ Law