Non-competitive inhibitors?

Question

How do non-competitive inhibitors change the shape of an enzyme once they've binded with its binding site?

Answer 1

Enzymes are made of protein. As we know that any of the amino acid residue being change would give rise to a different amino acid and the amino acid can give rise to a change in the shape of the entire protein.

With that in mind, we do know that when protein binds onto something, it would "change" or "twist" around to find the active site to bind. (Lock and Key theory) So, when a non-competitive inhibitor binds onto a protein, it would bind to a site whereby the protein has to "twist" and then allow a binding. This changes the entire shape of the enzyme.

Hope this helps.

Answer 2

Non competitive inhibitors do not directly compete with the substrate to bind to the enzymes active site. Instead they impede the enzymatic reactions by binding to the other part of the enzyme . This causes a shape change in the enzyme, causing the enzyme's active site to also change shape making it less affective at catalyzing a reaction.

Answer 3

when the inhibitor binds to the inhibitor site on the enzyme, new electrostatic attractions and hydrogen bonds form between the side chains in the amino acid sequence and the inhibitor. this results in an over all change in the protein's structure

Answer 4

A competitive inhibitor competes for the active site of an enzyme with the substrate molecules. A non-competitive inhibitor binds to the allosteric site of the enzyme, changing the shape of the active site. Do you need more detail?

Answer 5

First, Non competetitive inhibitors do not bind at the binding site, they bind at a site adjacent to the binding site.

Answer 6

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Answer 7

http://en.wikipedia.org/wiki/Enzyme_inhibitor