focus chapter 7 (kinetics and enzyme regulation) Flashcards
express a simple chemical reaction using the basic chemical rate law.
o A —K—-> B
o V=k[A]
A= reactant
B= product
K=rate constant
V=reaction rate or velocity
List three main assumptions of Michaelis-Menten kinetics.
-The steady-state assumption: [ES] is constant
-Free ligand approximation: valid as long as [E] is well below KM
-Rapid equilibrium approximation: substrate binding and dissociation occurs more rapidly than product formation
Km
- the ability of an enzyme to bind the substrate
Loosely related to the affinity of the enzyme for substrate (a dissociation constant)
Unique for each enzyme-substrate pair
The substrate concentration at which the reaction velocity is half-maximal
Kcat
-the ability of an enzyme to catalyze a reaction
varies for each substrate with an enzyme
turnover number of the enzyme
number of substrate molecules turned over to product molecules by the enzyme per unit time
number of reaction processes (turnovers) that each active site catalyzes per unit time.
Vmax
The maximum velocity of an enzymatically catalyzed reaction when the enzyme is saturated with its substrate
catalytic efficiency (kcat/Km)
A large kcat/KM ratio can arise from either a large kcat or a small KM (tight binding)
Michaelis-Menten plot
records the velocity of a reaction with increasing concentration of substrate
Lineweaver-Burk plots
Use data from M-M experiment and generate a double reciprocal plot