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Enzyme Inhibition: Types and Mechanisms

The document discusses two types of enzyme inhibition: irreversible and allosteric. Irreversible inhibitors permanently bind to enzymes via covalent bonds, leading to a permanent loss of activity, while allosteric inhibitors bind non-covalently to a different site, causing temporary changes in enzyme shape and activity. Key differences include binding site, bond type, reversibility, and physiological roles.

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9 views3 pages

Enzyme Inhibition: Types and Mechanisms

The document discusses two types of enzyme inhibition: irreversible and allosteric. Irreversible inhibitors permanently bind to enzymes via covalent bonds, leading to a permanent loss of activity, while allosteric inhibitors bind non-covalently to a different site, causing temporary changes in enzyme shape and activity. Key differences include binding site, bond type, reversibility, and physiological roles.

Uploaded by

debsekharmondal74
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd

Enzyme Inhibition: Irreversible vs Allosteric

Enzyme Inhibition - Overview

Enzyme inhibitors are molecules that decrease or block enzyme activity. They are generally

classified into:

- Reversible inhibitors (competitive, non-competitive, uncompetitive)

- Irreversible inhibitors

- Allosteric inhibitors

1. Irreversible Inhibition

Definition:

Irreversible inhibition occurs when an inhibitor binds permanently to an enzyme, usually forming

covalent bonds.

Mechanism:

- Inhibitor forms covalent bond at the active site

- Enzyme activity is permanently lost

Key Characteristics:

- Binding type: Covalent

- Reversibility: Irreversible

- Effect on Vmax: Decreases

- Effect on Km: Variable

- Recovery: Only by new enzyme synthesis

Examples:

- Aspirin (inhibits COX enzyme)


- Penicillin (inhibits transpeptidase)

- Organophosphates (inhibit acetylcholinesterase)

- Iodoacetate (inhibits glycolytic enzyme)

2. Allosteric Inhibition

Definition:

Allosteric inhibition occurs when an inhibitor binds to a site other than the active site, altering the

enzyme's shape.

Mechanism:

- Non-covalent binding at allosteric site

- Conformational change reduces enzyme activity

Key Characteristics:

- Binding site: Allosteric site

- Binding type: Non-covalent

- Reversibility: Reversible

- Effect on Vmax: Decreases

- Effect on Km: May or may not change

- Role: Feedback regulation

Examples:

- ATP (inhibits PFK-1 in glycolysis)

- CTP (inhibits aspartate transcarbamoylase)

- Isoleucine (inhibits threonine deaminase)

Irreversible vs Allosteric Inhibition - Comparison


Feature | Irreversible Inhibition | Allosteric Inhibition

---------------------|-----------------------------|------------------------------

Binding Site | Active site | Allosteric site

Bond Type | Covalent | Non-covalent

Reversibility | No | Yes

Effect on Enzyme | Permanently inactivates | Temporarily reduces activity

Physiological Role | Drug-related or toxic | Regulatory (metabolism)

Recovery | New enzyme needed | Reversible after removal

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