Level Biology Coursework Enzymes

This lets the hemoglobin release the oxygen for your tissues to use.Without it, hemoglobin wouldn't release oxygen as effectively and you would get less oxygen delivered to those cells that need oxygen to make energy.If you're making more energy, you need more oxygen to do so.

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We'll also go over some examples of allosteric regulation in the body.

Have you ever played with Legos or building blocks as a kid?

There are two forms of hemoglobin, the T state (or tense state), which makes hemoglobin bind oxygen less tightly, and the R state (or relaxed state), which makes hemoglobin bind oxygen more tightly.

Now, this might give you the impression that the T state is bad since it prevents hemoglobin from binding oxygen.

Since 2,3 BPG makes hemoglobin less likely to bind oxygen, it's considered an allosteric inhibitor, even though it does good things for our body.

Now, let's look at some examples of some allosteric activators.

These molecules and the allosteric site to which they bind are like the 'off switch' for the enzyme.

Allosteric activators on the other hand, make the enzyme more efficient.

They change the shape of the enzyme, like allosteric inhibitors, but they make the enzyme better able to bind the substrate, instead of worse. These molecules and their allosteric sites are like the 'on switch' for the enzyme.

Next, let's look at a few examples of how allosteric inhibitors and activators affect the allosteric site and enzyme activity.


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