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Law of Mass Action

Kinetics and Equilibria


As the reactants A & B are converted into the products P & Q
the rate of the forward reaction drops and that of the
backward reaction rises. Eventually, at equilibrium, both
rates are equal and the reaction appears to stop.
k1[A][B] = k-1[P][Q] k1 [P][Q]
= =K
k !1 [A][B]
K is the equilibrium constant

How can you improve concentration of product achievable?

Equilibrium Catalysis

• Overall free energy change • Enzymes catalyse reactions, ie


provides the driving force for the they make reactions go faster
reactions – Increase rate of reaction
Go at 25o For reaction A↔ B
(kcal mole 1) Composition at equilibrium
• Catalyst concentration remains
A% B% unchanged
• ΔGO = – RT lnK
5 0.02 99.98 • Enzymes do not change the
• T will increase rate 2 3.3 96.7 equilibrium of reactions.
0.5 30.1 69.9
• T may also affect equilibrium 0 50.0 50.0 – No change to K (K is given by
thermodynamics, not by
Table 1. Relationship between ΔGo and reaction kinetics)
composition at equilibrium.

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Michaelis-Menten Kinetics 1 Michaelis-Menten Kinetics 2

k1 k2 k1 k2
E + S ES E + P E + S ES E + P
k -1 k -1
• E - enzyme; S - substrate: (ES) - enzyme-substrate complex; P - product
• k1 rate constant of the (ES) formation
• k-1 rate constant for reverse reaction, ie. rate of substrate formation due to (ES) breakdown (2) Assume steady-state: [ES] is constant
• k2 rate constant for product formation
d[ES]/dt = 0 = k1 [E] [S] - k-1[ES] - k2[ES]
Enzymes are catalysts. The enzyme (E) and its substrate (S) bind
together to form the activated intermediate (ES) which breaks down to
release the enzyme and product (P).
(3) Mass balance of all catalytic species, assuming [E0] (total amount of
(1) We assume that the product formation is irreversible, ie we are enzymes) is observable
concerned only with initial velocities of the product formation rate rp. [E0] = [ES] + [E]

rp = d[P]/dt = k2[ES]
(therefore rp often also referred to as v0)

Michaelis-Menten Kinetics 3 Michaelis-Menten Equation For Single


Substrate Kinetics

(take notes) (take notes)

k cat[E o ][S]
rp =
Km + [S]

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Michaelis-Menten Equation
Michaelis-Menten Plot: Hyperbola
note that v0= Vmax, when [S] is infinite, so: Vmax = kcat [E o ] (6) 1st order mixed order 0th order

Therefore:
Vmax [S] Michaelis-Menten equation (7)
v0 =
Km + [S] Despite the similarities in shape,
this graph is NOT a graph of the
concentration of product forming
over time.
Significance of parameters:

kcat (Turnover number) is the rate constant for the catalytic reaction.

Km (Michaelis constant) is the dissociation constant for ES under the initial velocity conditions.

kcat/Km (Specificity constant) is a measure of the specificity for competing substrates.


At low [S],
kcat (8)
v 0 = [E][S]
Km

Lineweaver-Burke Plot Lineweaver-Burke Plot

• Inversion of Michaelis-Menten Equation


Lineweaver-Burk plot

1/v0
slope = K m /Vmax
1/Vmax

1/[S]
-1/K m

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Competitive Inhibition Competitive Inhibition

• Inhibitor I binds to the acitve site of the enzyme,


Vmax same
thus I and S compete to bind
Km increases by 1 + [I]/KI

kcat [E o ][S]
Michaelis-Menten equation becomes: v0 =
Km &$%$1 + [I] / KI #!"! + [S]

Non-competitive Inhibition Non-competitive Inhibition


Inhibitor binds to enzyme, but not at the active site, hence binds E and ES.

S, Km k cat
E ES E + P
Vmax decreases by 1 + [I]/KI
I, KI I, KI
Km stays the same

S, Km Michaelis-Menten equation becomes


EI ESI
kcat [E o ][S]
v0 = &
$1 + [I] / KI ! (Km + [S])
#
$ !
% "

Rates can also be affected by environmental factors of T and pH.

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Resources

• http://www.wiley.com/college/pratt/0471393878/st
udent/animations/enzyme_kinetics/index.html
• Or google: biochemistry essential enzyme kinetics

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