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The Behavior of
Proteins: Enzymes
• - Change
• [ ] - Concentration in moles per liter
• t - Time © 2018 Cengage Learning. All Rights Reserved.
Enzyme Kinetics (continued 1)
A B P
Rate = = =
t t t
Rate A B
f g
Rate = k A B
f g
Rate = k A B
1 1
Not responsible
for free activation
energy lowering
• –Δ[ES]/Δt
• Negative sign denotes that the concentration of the
complex decreases as it breaks down
• k–1 - Rate constant for the dissociation of the ES
complex to regenerate enzyme and substrate
• k2 - Rate constant for the reaction of the complex to
give product and enzyme
© 2018 Cengage Learning. All Rights Reserved.
Michaelis–Menten Model (continued 2)
• Steady state: Condition in which the [ES] remains
constant in spite of continuous turnover
• Reached when the rate of formation of the ES equals
the rate of its breakdown
Δ ES Δ ES
=
Δt Δt
k1 E S = k1 ES + k2 ES
E = E T ES
E ES S
T
=
k1 + k 2
= KM
ES k1
Vinit = Vmax = k2 E T
Vmax S Vmax
V = V =
S + S 2
• Random mechanism
1 K M + S 1 KM S
= =
V Vmax S V Vmax S Vmax S
1 KM 1 1
=
V Vmax S Vmax
y mx + b
• Ester bonds
E + S ES or E + I EI
1+
I
KI
1
=
KM 1 1 1
1 + × +
V Vmax K I S Vmax
y = m × x + b
I Vmax
V =
1 + I /K I
max
Noncompetitive inhibition
1
=
KM I 1 1 I
1 + × + 1 +
V Vmax KI S Vmax KI
y = m × x + b
© 2018 Cengage Learning. All Rights Reserved.
Figure 6.18 - Lineweaver–Burk Plot of Enzyme Kinetics
for Noncompetitive Inhibition