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Types of Enzyme Inhibition Explained

1. The document describes three types of enzyme inhibition: competitive, non-competitive, and uncompetitive inhibition. 2. For competitive inhibition, the inhibitor binds to the active site and competes with the substrate. For non-competitive inhibition, the inhibitor binds elsewhere and reduces enzyme activity. For uncompetitive inhibition, the inhibitor binds and inactivates the enzyme-substrate complex. 3. Reaction rate expressions are derived for each type of inhibition. Competitive inhibition increases Km and decreases Vmax, while non-competitive and uncompetitive inhibition decrease Vmax without changing Km.

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29 views6 pages

Types of Enzyme Inhibition Explained

1. The document describes three types of enzyme inhibition: competitive, non-competitive, and uncompetitive inhibition. 2. For competitive inhibition, the inhibitor binds to the active site and competes with the substrate. For non-competitive inhibition, the inhibitor binds elsewhere and reduces enzyme activity. For uncompetitive inhibition, the inhibitor binds and inactivates the enzyme-substrate complex. 3. Reaction rate expressions are derived for each type of inhibition. Competitive inhibition increases Km and decreases Vmax, while non-competitive and uncompetitive inhibition decrease Vmax without changing Km.

Uploaded by

ViaTS13
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

1

[Link]

Enzyme inhibition.
Instructor: Nam Sun Wang
Enzyme inhibition can be classified into the following three categories, depending on the mechanism.
Competitive
... The inhibitor binds to the active site and competes with the substrate.
Non-competitive ... The inhibitor binds to a different site and reduces enzyme activity.
Un-competitive ... The inhibitor binds to and inactivate the enzyme-substrate complex.
Derivation of Reaction Rate Expression with Equilibrium Assumption .
1. Competitive Inhibition.
Km

k2

E + S ES E + P
KI
E + I EI (inactive)
Given

1. dp/dt=rate=v
2. Conservation of enzyme species

v k 2 . ES
E 0 E EI
S. E

3. Equilibrium Assumption:

ES
K m. K I.
E 0 . K m.
Find( E , EI , ES , v )
K I. E 0 .

k 2. E 0. S
K m. 1

I
KI

v mapp. S
S

K mapp

E. I

Km

EI

KI

E0
K m. I

K I. K m

K I. S

K m. I

I
.
KI Km

K I. S

K m. I

S
K I. K m

K I. S

k 2 . K I. E 0 .

ES

K m. I

S
K I. K m
where

K I. S
v mapp k 2 . E 0 v m
K mapp K m. 1

I
KI

no change
As I , Kmapp .

[Link]

2. Non-competitive Inhibition.
Km

k2

E + S ES E + P
+
+
I
I
KI
KI
EI + S EIS
Km
Given 1. dp/dt=rate=v

v k 2 . ES
E 0 E EI

2. Conservation of enzyme species

S. E

3. Equilibrium Assumption:

K m. K I.
E 0 . K m.
E 0.

Find( E , EI , EIS , ES , v )

K m. I

K I. K m

S. I

S. K I

KI

EI

K I. K m

S. I

K I. S

K m. I

I
K I. K m

S. I

K I. S

S
K I. K m

S. I

K I. S

.I

S
K m. I

K I. K m

K m. I
k 2. E 0. S

k 2 . K I. E 0 . S

EIS

K m. I

k 2 . K I. E 0 .

E. I

KI

E0

K m. I

K I. E 0 .

ES

ES. I

Km

ES

EIS

I .
Km

S. I

S
.
KI Km

K I. S

S. I

K I. S

v mapp. S
S

K mapp

KI

where

v mapp

k 2. E 0
I

KI
K mapp K m

vm
1

As I , vm .

KI
no change

[Link]

3. Un-competitive Inhibition.
Km

k2

E + S ES E + P
KI
ES + I ESI (inactive)
Given

1. dp/dt=rate=v
2. Conservation of enzyme species

v k 2 . ES
E 0 E ESI
S. E

3. Equilibrium Assumption:

ES
K m. K I.
E 0 . S.

S. I
S. I

k 2. E 0. S
Km

S. 1

v mapp. S
I

K mapp

K I. K m
I
K I. K m

S. I

k 2 . K I. E 0 .

ES. I

Km

ESI

KI

E0

Find( E , ESI , ES , v )
K I. E 0 .

ES

K I. S
K I. S

S
K I. K m

K I. S

S
S. I

K I. K m
where

K I. S
v mapp

k 2. E 0
1

KI

I
KI
Km

K mapp
1

I
KI

vm
1

As I , vmapp .

KI
As I , Kmapp .

[Link]

Velocity and Lineweaver-Burk Plots


1. Competitive Inhibition.
vm

Km

KI

v m. S

v( S , I )

K m. 1
s

0.1 , 0.2 .. 10

KI

40

1
30
v( s , 0 )

v( s , 0 )

1
20
v( s , 1 )

v( s , 1 ) 0.5
v( s , 2 )

1
v( s , 2 ) 10

0
0

10

10

1
s

I=0
I=1
I=2

Common intercept; increased slope.

Substrate inhibition results when the inhibitor is the substrate, I=S


0.6

15

0.4

1
10
v( s , 0 )

0.2

1
v( s , s ) 5

v( s , s )

0
0

10

10

1
s

v is the same saturation curve, with reduced vm and

Increased intercept; common slope.

reduced K m. Competitive inhibition of substrate by


substrate is the same as no competitive inhibition at all;
a given substrate molecule is always in competition
with other substrate molecules.
v m. S

v
Km

Km
KI

v mapp. S
1 .S

K mapp

where

v mapp

vm
Km
KI

K mapp
1

Km
Km
KI

[Link]

2. Non-competitive Inhibition.

v m. S

v( S , I )
1

I .
Km
KI

40

1
30
v( s , 0 )

v( s , 0 )

1
20
v( s , 1 )

v( s , 1 ) 0.5
v( s , 2 )

1
v( s , 2 ) 10

0
0

10

10

1
s

I=0
I=1
I=2

Increased intercept & slope.

Substrate inhibition results when the inhibitor is the substrate, I=S


0.3

15

0.2

1
10
v( s , 0 )

0.1

1
v( s , s ) 5

v( s , s )

0
0

5
s

10

5
1
s

10

v curves downward at high value of s


v m. S
v
S term in the numerator, but quadratic S 2 term in the denominator.
S .
1
Km S
KI

6
3. Un-competitive Inhibition.

[Link]
v m. S

v( S , I )
Km

S. 1

I
KI

15

1
v( s , 0 ) 10

v( s , 0 )

1
v( s , 1 )

v( s , 1 ) 0.5
v( s , 2 )

1
5
v( s , 2 )

0
0

10

10

1
s

I=0
I=1
I=2

Increased intercept; common slope.

Substrate inhibition results when the inhibitor is the substrate, I=S


0.4

15

0.3

1
10
v( s , 0 )

v( s , s ) 0.2
1
v( s , s ) 5

0.1
0

0
0

5
s

10

10

1
s

v curves downward at high value of s


v m. S
S term in the numerator, but quadratic S 2 term in the
v
1 . 2 denominator. Thus, substrate inhibition via the non-competitive
Km S
S
inhibition mechanism cannot be distinguished from that from the
KI
uncompetitive inhibition mechanism.

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