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BioChem 6
BioChem 6
Campbell
Shawn O. Farrell
http://academic.cengage.com/chemistry/campbell
Chapter Six
The Behavior of Proteins: Enzymes
Enzyme Catalysis
Enzyme: a biological catalyst
H2 O +
O2
Enzyme Kinetics
For the reaction
A + B
D[P]
=
Dt
C + D
+ HPO 42-
Glucose-1-phosphate + Glycogen
24 ]
n-1
ES
enzyme-substrate
complex
Binding Models
Two models have been developed to describe
formation of the enzyme-substrate complex
Lock-and-key model: substrate binds to that portion
of the enzyme with a complementary shape
Induced fit model: binding of the substrate induces a
change in the conformation of the enzyme that results
in a complementary fit
Formation of Product
Michaelis-Menten Kinetics
Initial rate of an enzyme-catalyzed reaction versus
substrate concentration
Michaelis-Menten Model
For an enzyme-catalyzed reaction
k1
E + S
k-1
ES
k2
-1 [ES]
+ k2[ES]
k-1 + k2
= KM
k1
= KM
Or alternatively
[ES]
[E] T [S]
=
KM + [S]
Vinit = k2 [ES]
k 2[E]T [S]
=
KM + [S]
Vinit =
Vmax [S]
KM + [S]
Michaelis-Menten
equation
V=
Vmax [S]
KM + [S]
Vmax [S]
[S] + [S]
Vmax
2
V=
Vmax [S]
KM + [S]
1
V
1
V
KM + [S ]
Vmax [S ]
KM
Vmax [S ]
KM
Vmax [S ]
1
Vmax
[S ]
Vmax [S ]
Lineweaver-Burk Plot
The Lineweaver-Burke plot has the form y = mx + b, and is the
formula for a straight line
1
V
KM
=
Vmax
[S ]
1
Vmax
b
a plot of 1/V versus 1/[S] will give a straight line with slope of
KM/Vmax and y intercept of 1/Vmax
such a plot is known as a Lineweaver-Burk double reciprocal
plot
Turnover Numbers
Vmax is related to the turnover number of enzyme:also
called kcat
V max
Enzyme Inhibition
Reversible inhibitor: a substance that binds to an enzyme to inhibit it, but
can be released
Competitive Inhibition
Substrate must compete with inhibitor for the active
site; more substrate is required to reach a given
reaction velocity
EI
+ E + S
ES
EI
KI =
[E][I]
[EI]
Competitive Inhibition
Competitive Inhibition
No inhibition
1 = KM
V
Vmax
m
y =
1
S
1
Vmax
b
KM
Vmax
1 +
m
[I]
KI
1
S
1
Vmax
b
E
-I
ES
E + P
-S
+I
-I
+S
EI
+I
ES I
-S
max =
Vmax
1 + [I]/K I
No inhibition
1 = KM 1
S
V
Vmax
1
Vmax
x + b
In the presence of a noncompetitive inhibitor
y =
1
V
KM
Vmax
1 +
m
[I]
KI
1
S
1
Vmax
1 +
[I]
KI