I am sooooo lost in my bio class, can anyone explain to me what are enzyme inhibitors?

Answer 1

Simple version: an enzyme is something that makes a chemical reaction go better... and enzyme inhibitor is something that makes it harder for the enzyme to do whatever it was doing.

There are a lot of ways these inhibitors can work.

- Some clamp onto the enzyme and change it in such a way that it is harder or incapable of doing its job (like putting ice cream in your DVD player).
- Some just look a lot like what the enzyme is supposed to effect so the enzyme wastes a lot of time looking for the right stuff (like hiding your favorite movie DVD in a stack of DVD recordings of congressional subcommittees).

...and there are even variations within those. Putting ice cream in your DVD would probably be a pretty permanent way of inhibiting it (and some inhibitors do permanantly affect enzymes), but we might also just smear ice cream on the DVDs so you'd have to clean them before watching (and some inhibitors are temporary or reversible in this way).

But the bottom line is just that inhibitors mess up enzymes. Sometimes that's even a wonderful thing to happen (if you're messing up a virus) as opposed to a bad thing (the virus is messing up you).

Answer 2

Enzyme inhibitors deactivate the enzyme by attaching to an allosteric site, a part on the enzyme away from the active site. This binding to the allosteric site changes the shape of the active site. The active site is then incompatible with the molecule it is supposed to catalyze since the shapes of the active site and the molecule do not fit like a lock and key. When the inhibitor leaves the allosteric site, the active site then resumes its orginial shape and can then bind once more with the molecule it is supposed to catalyze.

Answer 3

Enzyme inhibitors deactivate the enzyme by attaching to an allosteric site, a part on the enzyme away from the active site. This binding to the allosteric site changes the shape of the active site. The active site is then incompatible with the molecule it is supposed to catalyze since the shapes of the active site and the molecule do not fit like a lock and key. When the inhibitor leaves the allosteric site, the active site then resumes its orginial shape and can then bind once more with the molecule it is supposed to catalyze.

Answer 4

Essentially, they're molecules that inhibit the functions of their target enzymes by either blocking or modifying the active sites thru structure or charges. Inhibitors can be weakly binded to enzymes via hydrogen bonds for example or strongly binded via covalent bonds.