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Kinetics
Learning Objectives for Theme 2 Topic B Energy & Metabolic Pathways
Review Enzymes
Nearly every reaction that occurs in living organisms is catalyzed
by an enzyme.
Enzymes vastly increase the rate of reaction by decreasing G*
(E*, EA, G0,).
Enzymes are quite specific and catalyze only one reaction.
Review of Enzyme function
http://www.youtube.com/watch?v=E-_r3omrnxw&feature=related
Many bio-reactions look like coupled reactions.
Enzymes catalyze the two coupled reactions simultaneously.
Often one of the coupled reactions is ATP + H2O ADP + Pi
Therefore: Enzymes look like energy coupling devices.
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Example Reaction
CPRG(aq) + H2O(aq) CPR(aq) + galactose
Lactaid, is an enzyme supplement (beta-glactosidase)
(CPRG = Chlorophenolred-galactoside)
Example:
A572 = 0.44 umoles of Product after 2.0 minutes.
Velocity = 0.44 umoles / 2.0 minutes = 0.22 umol/min.
All of these
tubes have have
the same [S] but
they have
different [E].
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All of these
tubes have have
the same [E] but
they have
different [S].
Substrate
10
Km 4.0 uM
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No Inhibitor
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Competitive Inhibitor
Inhibitor looks chemically somewhat like the substrate.
Inhibitor binds at the active site in competition with the substrate.
High concentrations of the substrate will out-compete the inhibitor.
Active
Site
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Noncompetitive Inhibition
Inhibitor is not chemically similar to the substrate.
Inhibitor binds at some other site on the enzyme (not the active site).
High concentrations of the substrate do not out-compete the inhibitor.
Active
Site
Inhibitor
Site
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Reversible Inhibition
Competitive Inhibition is one type of Reversible Inhibition because the
inhibitor can be released from the enzyme.
o High [S] will knock the inhibitor off of the enzyme Vmax is unchanged
Non-Competitive Inhibition is another type of Reversible Inhibition.
o High [S] will not knock the inhibitor from the E Vmax is decreased.
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Irreversible Inhibition
Inhibitor reacts with the enzyme so that the enzyme doesnt catalyze
properly.
The substrate can NOT out-compete so that Vmax is decreased.
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5.1 What is a common way to obtain the data needed to calculate the
velocity of an enzyme catalyzed reaction?
A. Measure the heat released by the reaction.
B. Measure the equilibrium constant after the reaction has stopped.
C. Measure the decrease in the substrate concentration.
D. Measure the absorbance of the products.
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5.2 How does the velocity (v) of an enzyme catalyzed reaction depend on [E]
and [S]?
A. v increases linearly with both increasing [E] and increasing [S].
B. v does not increase linearly with either [E] or [S].
C. v increases linearly with increasing [E], but reaches a plateau with
increasing [S].
D. v increases reaches a plateau with increasing [E], increases linearly with
increasing [S].
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