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An enzyme, E, combines with S to form an ES complex, with a rate constant k1. The ES
complex has two possible fates. It can dissociate to E and S, with a rate constant of k-1,
or it can proceed to form product, P, with a rate constant k2.
Michaelis and Menten made a derivation of these kinetic characteristics to arrive at the
Michaelis-Menten Equation:
Vinit =
Vmax [S]
KM + [S]
Mi chael is-Menten
equation
k1
k-1
ES
k2
-1 [ES]
+ k 2[ES]
k-1 + k2
= KM
k1
Or alternatively
[E]T [S]
[ES] =
KM + [S]
Vinit = k 2 [ES]
k 2[E]T [S]
=
KM + [S]
Vinit =
Vmax [S]
KM + [S]
Mi chael is-Menten
equation
The [S]=
Meaning
KM orreduces
the Michaelis
constant
When
KM, the of
equation
to
V=
Vmax [S]
KM + [S]
Vmax [S]
[S] + [S]
Vmax
2
KM + [S]
KM + [S]
Vmax [S]
KM
+
=
Vmax [S]
1
V
1
V
KM
+ 1
=
Vmax [S]
Vmax
[S]
Vmax [S]
Lineweaver-Burk Plot
1 form
1 + b, and is the
The Lineweaver-Burke
the
y = mx
1 = KMplot has
+
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
Double reciprocal plots can easily be understood and provide
recognizable pattern for the study of ENZYME INHIBITION
KLineweaver-Burk
M is the
dissociation
constant for ES; the
greater the value of
KM, the less tightly S
is bound to E
Plot (Contd)
Turnover Numbers
Vmax is related to the turnover number of enzyme:also
called kmax
cat
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
I + E + S
ES
P
KI =
[E][I]
[EI]
Competitive Inhibition
Competitive
Inhibition
No inhibiti
on
y =
KM
Vmax
m
1
V
1
S
1
Vmax
b
KM
Vmax
1 +
[I]
KI
1
S
1
Vmax
b
-I
ES
-S
+I
-I
+S
EI
+I
ESI
-S
max
Vmax
1 + [I]/KI
E + P
1
V
KM
Vmax
1 +
m
[I]
KI
1
S
+
+
1
Vmax
1 +
b
[I]
KI
Uncompetitive Inhibition
Uncompetitive Inhibition
Summary
Effects Type
of reversible
inhibitors on kinetic
constants
of Inhibitor
Effect
Competitive (I binds to E only)