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Module 5 Inhibition Kinetics

The document discusses the three major classes of reversible enzyme inhibition: competitive, uncompetitive, and mixed inhibition. It details the mechanisms of each type, including the specific characteristics of mixed and non-competitive inhibition, as well as their effects on enzyme kinetics. Additionally, it presents problems and solutions related to competitive inhibition, including calculations of kinetic parameters.

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9 views22 pages

Module 5 Inhibition Kinetics

The document discusses the three major classes of reversible enzyme inhibition: competitive, uncompetitive, and mixed inhibition. It details the mechanisms of each type, including the specific characteristics of mixed and non-competitive inhibition, as well as their effects on enzyme kinetics. Additionally, it presents problems and solutions related to competitive inhibition, including calculations of kinetic parameters.

Uploaded by

ritmay008
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

Module 5

Inhibition Kinetics
The three major classes of reversible enzyme inhibition are competitive inhibition,
uncompetitive inhibition and mixed inhibition
COMPETITIVE ENZYME INHIBITION
COMPETITIVE ENZYME INHIBITION (Contd.)
COMPETITIVE ENZYME INHIBITION (Contd.)
UNCOMPETITIVE ENZYME INHIBITION
UNCOMPETITIVE ENZYME INHIBITION (Contd.)
UNCOMPETITIVE ENZYME INHIBITION (Contd.)
MIXED INHIBITION

 Mixed inhibitors are able to bind to both free enzyme and bound enzyme (ES
complex) alike at the allosteric site. The binding affinity of the inhibitor to the free
and bound enzyme can be different as presence of the substrate can lead to a
change in the structure of the allosteric site (where inhibitor binds).

 Hence, dissociation constant of the EI complex (KI) may not be the same as
dissociation constant of the ESI complex (KI’) during mixed inhibition.

 One special case of mixed inhibition is non-competitive inhibition where the


inhibitor has same binding affinity to free as well as bound enzyme. Hence, KI=KI’
for non-competitive inhibition.
NON-COMPETITIVE INHIBTION
NON-COMPETITIVE INHIBTION (Contd.)

The net effect of non-competitive inhibition is a reduction in vm


NON-COMPETITIVE INHIBTION (Contd.)
• Similarly, penicillin is an irreversible inhibitor of D-D transpeptidase, an
enzyme involved in bacterial peptidoglycan synthesis.
Problem 1
Solution

1.6
I= 1.26 mM
1.4 y = 0.309x + 0.1619
1.2
1
y = 0.194x + 0.1578
1/V

0.8
0.6 I= 0 mM
0.4
0.2
0
0 1 2 3 4 5
1/S

a) Competitive inhibition

a) Km= 1.23 mM
vm= 6.17 mM
KI = 2.28 mM
Problem 2

Units for v is g/[Link]


Solution

5
4.5 y = 9.5225x + 0.601
4
3.5
3

1/V
2.5
2
1.5
1
0.5
0
0 0.1 0.2 0.3 0.4 0.5
1/S

a) Competitive inhibition
b) Ki= 1.38 g/L
FACTORS AFFECTING ENZYME REACTIONS
FACTORS AFFECTING ENZYME REACTIONS (Contd.)

The descending portion of the plot is due to the


enzyme denaturation.
FACTORS AFFECTING ENZYME REACTIONS (Contd.)

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