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Vinit =
Vmax [S]
KM + [S]
Michaelis-Menten
equation
k1
k-1
ES
k2
(cont.)
k-1 + k2
k1
= KM
(cont.)
Or alternatively
[ES]
[E] T [S]
=
KM + [S]
(cont.)
Vinit = k2 [ES]
k 2[E]T [S]
=
KM + [S]
Vmax [S]
KM + [S]
Michaelis-Menten
equation
= KM
[E]Taffinity
[S] - [ES][S]
= KS:
M[ES]
of E for
if k2 is <k-1 or k1,
A measure of the
neglecting k2, therefore[E]
KMT [S]
= k=-1/k
1
[ES](K
M + [S])
V=
Vmax [S]
KM + [S]
Vmax [S]
[S] + [S]
Vmax
2
Vmax [S]
V=
KM + [S]
1 =
V
KM + [S]
Vmax [S]
KM
Vmax [S]
KM
1 =
+ 1
V
Vmax [S]
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
Turnover Numbers
Vmax is related to the turnover number of
enzyme:also called kcat
V max
Enzyme Inhibition
Competitive Inhibition
o Substrate must compete with inhibitor for the
active site; more substrate is required to reach a
given reaction velocity
EI
+ E + S
ES
+ E
KI =
[E][I]
[EI]
Competitive Inhibition
Competitive Inhibition
No inhibition
1 = KM
V
Vmax
y =
1
S
Vmax
b
1
S
Vmax
b
E
-I
ES
-S
+I
-I
+S
EI
-S
E + P
+I
ESI
max =
Vmax
1 + [I]/K I
Vmax
y =
m x + b
In the presence of a noncompetitive inhibitor
1 = KM 1 + [I]
V
Vmax
KI
1
S
Vmax
1 +
b
[I]
KI
Uncompetitive Inhibition
Uncompetitive Inhibition
Summary
Effects of reversible inhibitors on kinetic constants
Type of Inhibitor
Effect
Competitive (I binds to E
only)
Uncompetitive (I binds to
ES only)
Non-competitive (I binds to
E or to ES)
Lowers Vmax; KM
unchanged