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For allosteric inhibition, the inhibitor binds to the enzyme and induces a change in the conformation so that the substrate cannot bind anymore. The binding site for the allosteric inhibitor is different from the substrate, see the image for illustration (from here): In non-competetive inhibition the inhibitor also binds to the enzyme indepently of the ...


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Aspirin and some other NSAIDs inhibit cyclooxygenase which is the first enzyme in the prostaglandin/thromboxane biosynthesis pathway if you consider first substance is arachidonic acid (a fatty acid). Generally, arachidonic acid is present in the form of a phospholipid, and if you consider that in the pathway, substance-Y is arachidonic acid and enzyme-A is ...


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Apart from what Phototroph mentioned in their answer (competitive and non-competitive inhibition), an enzyme can be activated/inhibited via covalent modification of the protein (post-translational modification) such as phosphorylation by protein kinases (phosphorylation is the most common modification).


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Yes, competitive inhibition is another form of enzyme inhibition. The inhibitor binds to the active site here, as opposed to allosteric inhibition, where it binds to a secondary site. An example of an inhibitor would be the cyanide ion (CN-), which inhibits Cytochrome C oxidase, preventing electron chain transport and thus ATP production. Note this ion is ...



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