This preview shows pages 1–3. Sign up to view the full content.
ENZYME KINETICS
Transformations of the MichaelisMenten Equation
0
1 10
5
2 10
5
3 10
5
4 10
5
5 10
5
0
5
10
15
20
25
v
0
(s
1
)
[S]
0
(mM)
K
M
V
max
/2
What is the approximate V
max
for this enzyme?
4.5 x 10
5
What is the approximate K
M
for this enzyme?
5 μM
The MM Equation can be transformed
to provide more accurate information
1. Standard MM Equation
v
0
=
V
max
S
[ ]
K
M
+
S
[ ]
2. Take the inverse of both sides
1
v
0
=
K
M
+
S
[ ]
V
max
S
[ ]
3. Separate into two parts and simplify
1
v
0
=
K
M
V
max
S
[ ]
+
S
[ ]
V
max
S
[ ]
1
v
0
=
K
M
V
max
S
[ ]
+
1
V
max
1
v
0
=
K
M
V
max
⎛
⎝
⎜
⎞
⎠
⎟
1
S
[ ]
+
1
V
max
Linear
transformation of
the MM equation!
1
v
0
=
K
M
V
max
⎛
⎝
⎜
⎞
⎠
⎟
1
S
[ ]
+
1
V
max
y
=
m
•
x
+
b
±
a plot of 1/v
0
vs 1/[S] yields a straight line
±
the slope is K
M
/V
max
±
the yintercept is 1/V
max
±
the xintercept (set y = 0) = 1/K
M
This preview has intentionally blurred sections. Sign up to view the full version.
View Full Document1
v
0
=
K
M
V
max
⎛
⎝
⎜
⎞
⎠
⎟
1
S
[ ]
+
1
V
max
v
0
=
V
max
S
[ ]
K
M
+
S
[ ]
[S] (mM)
v
0
(μM•s
1
)
1
2.5
2
4.0
7
6.3
10
7.6
20
9.0
2
3
4
5
6
7
8
9
10
0
5
10
15
20
25
v0 (
µ
M•s1)
v
0
(
µ
M•s
1
)
[S] (
µ
M)
1/[S]
1/v
0
1
0.4
0.5
0.25
0.2
0.16
0.1
0.13
0.05
0.11
0.1
0.15
0.2
0.25
0.3
0.35
0.4
0.45
0
0.2
0.4
0.6
0.8
1
1.2
1/v0
y = 0.10419 + 0.29589x
R= 0.99803
1/v
0
1/[S]
1
v
0
=
K
M
V
max
⎛
⎝
⎜
⎞
⎠
⎟
1
S
[ ]
+
1
V
max
yintercept = 0.104
xintercept = 1/K
M
y =
0.296x
+ 0.104
0.1
0.15
0.2
0.25
0.3
0.35
0.4
0.45
0
0.2
0.4
0.6
0.8
1
1.2
1/v0
y = 0.10419 + 0.29589x
R= 0.99803
1/[S]
= 1/V
max
V
max
= 9.615 μM•s
1
= 1/0.35
K
M
= 2.8μM
(set y=0 in the equation)
Reversible Inhibition
This is the end of the preview. Sign up
to
access the rest of the document.
This note was uploaded on 11/28/2011 for the course CHEM 340 taught by Professor T.baird during the Fall '11 term at S.F. State.
 Fall '11
 T.Baird
 Chemistry, Enzyme, Kinetics

Click to edit the document details