Section 5.8: Irreversible Inhibition
- Like reversible inhibition, irreversible inhibition reduces the activity of an enzyme.
- However, as the name implies, it is more permanent because it usually involves the formation of a covalent bond
between the inhibitor and the enzyme
- Often, the reaction is an alkylation or acylation of a side chain of an amino acid residue
in the enzyme
- A common feature of many irreversible inhibitors is that they resemble the natural substrate of
the enzyme, so that they bind as substrate analogs
- In addition, they often form bonds with especially reactive groups in the active site of an enzyme
(eg: the catalytic serine residue of a serine protease)
- Consequently, these kinds of inhibitors are found in toxins and can be used
for analytical purposes