MCB Lec 10

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1
Enzyme Kinetics
the study of reaction rates that are catalyzed by a purified enzyme
2
Michaelis Menten Equation
V0= (vmax[S]) / (Km + [S])
3
Binding Step
forward is K1, backward is K-1
E+S <---> ES
4
Catalytic step
kCat (turnover number)
ES --> E+P
5
Lower Km indicates
tighter and higher affinity for ES
6
Kcat
# of molecules in a given time when enzyme is saturated with substrate
7
We assume that ES is _______ in the Michaelis Menten Equation
constant
8
Michaelis Constant formula
Km= (k-1+ kcat) / k1
9
Y intercept and X intercept of Lineweaver-Burk plot
Y intercept = 1 / (V max)
X intercept = - 1 / Km
10
High Km
leads to enzyme being idle
11
vmax
max velocity
12
Km
substrate concentration that is needed to achieve half of Vmax
13
Kcat/Km: : catalytic efficiency
The ratio Kcat/Km combines information about how fast bound substrate is processed and how well substrate is captured
14
Catalytic Perfection
- every collision between enzyme and its substrate is productive
- the rate is only limited by the frequency of collision between the enzyme and its substrates
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