Enzymes (Ross) Flashcards
At what values of ΔGo′ and Keq are the products favored?
ΔGo′ less than 0
Keq greater than 1
At what values of ΔGo′ and Keq are the reactants favored?
ΔGo′>0
Keq less than 1
What is the equation for Gibb’s free energy?
ΔG=ΔGo′+RTlnKeq
Name the four different catalytic strategies
Covalent catalysis
General acid-base catalysis
Catalysis by approximation
Metal ion catalysis
What is the Michaelis-Menten equation?
Vo=Vm[S]/(Km+[S])
What relation describes the fraction of active sites filled?
[ES]/[E]total=Vo/Vm=[S]/(Km+[S])
What are the assumptions of the Michaelis-Menten equation?
- Formation of ES complex
- No back reaction from product buildup i.e. k4=0
- Initial velocities used for analysis
- Steady state assumption for [ES]
- Negligible depletion of substrate i.e. [S]>[E]
Define the Michaelis constant Km
Km=(k2+k3)/k1
Define the turnover number and what it measures
Turnover number=k3=kcat
Measure of the catalytic ability of the enzyme when the active sites are saturated
Define catalytic efficiency
Kcat/Km
What is a perfect enzyme?
One whose catalytic efficiency is limited only by the rate of diffusion of the substrate to the enzyme
What the characteristics of the Lineweaver-Burk plot?
x-int=-1/Km
y-int=1/Vm
slope=Km/Vm
For two-substrate kinetics, name the three types of mechanisms
Ordered sequential
Random sequential
Ping-pong (double replacement)
Describe the changes in Vm, Km, and Kcat/Km for competitive inhibitors
Vm stays the same
Km increases
kcat/Vm decreases
Describe the changes in Vm, Km, and Kcat/Km for noncompetitive inhibitors
Vm decreases
Km stays the same
kcat/Vm decreases