Irreversible inhibitors: Difference between revisions
No edit summary |
m Irreversible inhibitors increase the affinity for the substrate on the enzyme, subsequently Km decreases. Irreversible inhibitors also leave Vmax unchanged. |
||
| Line 3: | Line 3: | ||
=== References === | === References === | ||
<references /> | <references />(Bruce Alberts: Molecuar Biology of the Cell; 6th edition, United states of America, Garland science) | ||
<div class="grammarly-disable-indicator"></div> | |||
Revision as of 12:15, 6 December 2017
An irreversible inhibitor will bind to an enzyme so that no other enzyme-substrate complexes can form. It will bind to the enzyme using a covalent bond at the active site which therefore makes the enzyme denatured. An example of an irreversible inhibitor is diisopropyl fluorophosphate which is present in nerve gas. It binds to the enzyme and stops nerve impulses being transmitted. An example of where we use irreversible inhibitors in medicine is penicillin. Penicillin works by inhibiting the activity of the enzyme responsible for the creation of the bacterial cell wall. This means that water can enter the bacterial cell, causing it to swell, burst and die termed lysis. [1]
References
- ↑ Becker's World of the Cell, J.Hardin, G.Bertoni, L.J.Kleinsmith,8th edition, Pearson Benjamin Cummings, p 145
(Bruce Alberts: Molecuar Biology of the Cell; 6th edition, United states of America, Garland science)