Biology Reference
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d
[
S
]
d
[
P
]
Differentiating both sides of this equation with respect to t yields
=
.
dt
dt
Hence, Eq. ( 2.14 ) becomes
d
[
S
]
V max [
S
]
=−
] .
(2.18)
dt
K m +[
S
The evolution of the substrate concentration can be simulated by solving this differen-
tial equation after fixing V max and K m and assigning a value to the initial concentration
of the substrate. Then, from Eq. ( 2.17 ), one can compute the progress curve for the
concentration of the product.
Exercise 2.1. Consider the reactions where two substrates S 1 and S 2 compete
for binding to an enzyme E to produce two different products P 1 and P 2 . Under the
assumption that each reaction follows theMichaelis-Menten kinetics, derive rate equa-
tions for P 1 and P 2 in this system and explain the effects of the competition occurring.
k 1
k 2
k 3
−→
E
+
S 1
ES 1
P 1 +
E
.
p 1
p 2
p 3
−→
E
+
S 2
ES 2
P 2 +
E
.
2.3.2 Multi-Molecule Binding and Hill Equations
Some enzymes react with more than one substrate molecule, e.g., the reaction in
Eq. ( 2.19 ), in which n -molecules of a substrate react with an enzyme E . For simplicity,
let's assume that the binding sides on the enzyme are all identical, the bindings take
place simultaneously and the bindings of n -molecules are independent. Otherwise,
the influence of each binding step to other binding steps has to be considered.
nS k 1
k 3
E
+
k 2 ES n
P
+
E
.
(2.19)
k 1
−→
This reaction consists of three individual reactions. In the first reaction, E
+
nS
n -molecules of a substrate S interact with one molecule of an enzyme E to form
an enzyme-substrate complex ES n with a rate constant k 1 . ES n
ES n ,
k 2
−→
nS is the
second reaction, in which the enzyme-substrate complex ES n can break down into the
enzyme E and n -substrate S molecules with a rate constant k 2 . In the third reaction,
ES n
E
+
k 3
−→
P , the enzyme E releases unchanged from the complex and a product
P is produced with a rate constant k 3 . The differential equation modeling dynamics
of the concentration of the enzyme-substrate complex ES n is the difference between
the production and consumption rates of this complex. ES n is produced with the first
reaction and it is used up with both the second and the third reactions. Hence,
E
+
[
ES n ]
dt
d
n
=
k 1 [
][
]
(
k 2 +
k 3 ) [
ES n ] .
E
S
(2.20)
 
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