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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 ...


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 ...


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).


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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