It
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Reversible
Competitive
Non- competitive
uncompetitive
Irreversible
Allosteric
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Cartoon Guide
Competitive
Non-competitive
Uncompetitive
E
Substrate
S
I
I
Inhibitor
Compete for
active site
E + S
ES E + P
+
I
EII
[II] binds to free [E] only,
and competes with [S];
increasing [S] overcomes
Inhibition by [II].
Different site
E + S
ES E + P
+
+
I
I
EII + S EIIS
[II] binds to free [E] or [ES]
complex; Increasing [S] can
not overcome [II] inhibition.
E + S
ES E + P
+
I
EIIS
[II] binds to [ES] complex
only, increasing [S] favors
the inhibition by [II].
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Competitive
Non-competitive
Vmax
Double Reciprocal
[S], mM
Km Km
Uncompetitive
Vmax
vo
Direct Plots
vo
Vmax
[S], mM
Km = Km
Vmax
Km Km
Vmax
[S], mM
Vmax unchanged
Km increased
Vmax decreased
Km unchanged
1/vo
1/vo
1/vo
Intersect
at Y axis
1/Km
Two parallel
lines
1/ Vmax
1/[S]
1/ Vmax
Intersect
at X axis
1/Km
1/[S]
1/ Vmax
1/Km
1/[S]
11
12
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13
ability or affinity
increases
-ve:- binding ability or affinity
decreases
14
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15
16
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Assumption
17
Specific activity:
Used to follow the increasing purity of an enzyme
through several procedural steps.
Molecular activity:
Used to compare activities of different enzymes.
Also called the turn-over number (TON = kcat)
18
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Specific activity:
mol substrate/min-mg E = unit/mg E
Molecular activity:
mol substrate/min- mol E = units/mol E
19
Temperature
pH
Concentration
Activators
Product
concentration
Time
Radiations
20
10
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Collision rate of
enzymes and
substrates
Number of
enzymes
remaining
undenatured
o
Temperature / C
21
Increasing kinetic
energy increases
successful collision
rate
Temperature / C
22
11
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Permanent disruption
of tertiary structure
leads to loss of active
site shape, loss of
binding efficiency and
activity
Temperature / C
23
Optimum temperature
Temperature / C
24
12
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The
26
13
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27
Optimum pH
14
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Optimum pH
pH
29
pH:
15
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31
32
16