Lineweaver-Burk's double reciprocal plot

Michaelis-Menten scheme
Vmax [S]
v0 = 1 = Km + [S] = Km 1 + 1
Km + [S] v0 Vmax [S] Vmax [S] Vmax this follows a
y = mx + b
formula

y m x b
slope y-intercept
1
an interesting graphical application:
v0 in bisubstrate systms, a Lineweaver-Burk plot can help to distinguish
y intercept is 1/Vmax whether a ping-pong mechanism (one substrate attached to the enzyme at a
* time) or ternary complex (ES1S2) forms during the catalytic event.
increasing S2 increasing S2
substrates meet
slope is Km/Vmax during the 1
mechanism 1 ping-pong v0
v0
* 1
substrates do
not meet
[S] *
x intercept is -1/Km
1 1
[S1] [S1]
Thinking about the intercepts:
When x = 0, 1/[S] approaches 0, or [S] is increasing to an infinite level,
it makes sense that Vmax is attained there (think of the end of the v0 vs [S] plot)
When y = 0, you are really thinking about the highest possible rate of reaction, but [S] can never be 0, much less
negative, so this is only a hypothetical situation we are taking advantage of in order to solve for these constants
(think of the beginning v0 vs [S] plot when S approaches 0 and the slopes of that initial linear part of the curve are
maximized)
Changing an enzyme's behavior by adding an inhibitor (i.e. a drug).
1 Compare the efficiencies of the original enzyme and the new one (dashed).
v0 The new plot has same Vmax but Km has increased (1/Km decreased)
worse enzyme - higher Km means it takes more [S] to be saturated, even
* though it ultimately can still attain the same Vmax
Efficiency is kcat/Km, so efficiency is lower
This effect would be seen if the enzyme were treated with a drug that competes
with substrate for the enzyme's active site (competitive inhibitors)
* 1
1
[S] v0 Lower Vmax and the same Km
Efficiency is lower
The new one affects * (noncompetitive inhibitors are
1
Km and Vmax very rare, usually seen in two-
v0
Seems as though Km substrate systems)
* 1

* decreases!
only because the drug
[S]
binds ES 1
Typically the result is a v0
Lower Vmax and higher Km
worse enzyme overall Efficiency is lower
*
* 1 (uncompetitive
inhibitors)
(mixed inhibitors because drug
binds to both ES and E) looks like
[S] a mix of non- and competitive
* 1
EXTREMELY common)
[S] Nolta 2009