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Equilibrium Catalysis
1
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)
k cat[E o ][S]
rp =
Km + [S]
2
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.
1/v0
slope = K m /Vmax
1/Vmax
1/[S]
-1/K m
3
Competitive Inhibition Competitive Inhibition
kcat [E o ][S]
Michaelis-Menten equation becomes: v0 =
Km &$%$1 + [I] / KI #!"! + [S]
S, Km k cat
E ES E + P
Vmax decreases by 1 + [I]/KI
I, KI I, KI
Km stays the same
4
Resources
• http://www.wiley.com/college/pratt/0471393878/st
udent/animations/enzyme_kinetics/index.html
• Or google: biochemistry essential enzyme kinetics