Meglimb
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#1
Report Thread starter 4 years ago
#1
Does anybody have any tips on enzyme inhibitors and examples for each one I just did I lesson on it by I don’t quite understand it .
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username3567284
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#2
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Well what exactly don't you understand about it?

Enzyme inhibitors basically prevent a substrate from being catalysed by an enzyme so it's reaction can't be completed.

There are 2 kind of inhibitors, competitive and noncompetitive. Competitive inhibitors block the enzyme's active site, so the natural substrate can't enter the active site of the enzyme, and therefore can't be catalysed by it. Noncompetitive inhibitors bind to the enzyme but not the active site; an allosteric site, this changes the shape of the active site so the substrate can't be catalysed.
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Meglimb
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#3
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#3
I dont understand poison and medicine inhibitors .
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James3000117
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#4
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They're just trying to get you to apply everything cosmicsnowflake said to specific examples. Any you need to memorise for the exam will be listed in your specification. Otherwise simply apply inhibitor theory to whatever weird thing they give you on the day. What sort of inhibition is occurring? What effect will this have on the body? How does this specific enzyme being inhibited lead to the effect the drug/poison has?

Some examples include cyanide, which irreversibly inhibits a respiratory enzyme, preventing ATP production. Obviously if no ATP can be produced the body is in a bit of trouble, hence why it's a poison. Statins are reversible competitive inhibitors that inhibit a cholesterol producing enzyme. Why is it important that they're reversible?

Some other examples you might be interested in (though probably won't have to memorise all the detail of) include organophosphates and aspirin (aspirin can get complicated, just an outline will do.)
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