VCE · Chemistry · Medicinal Chemistry live from the app

Enzyme Inhibition

Two ways to stop an enzyme. Competitive inhibitors fight for the active site and can be outcompeted by more substrate; non-competitive inhibitors bind elsewhere, deform the active site, and cannot. This is the real knowscape from knowhere, not a picture of one. Drag it. Watch what actually changes.

chemistry · medicinal chemistry · enzyme inhibitiondrag it · it is yours
the one idea

why this one carries the topic.

A drug works because its shape fits something in your body, and stops working when it doesn't. Everything about designing one comes back to that fit.

Competitive inhibitors structurally resemble the substrate and bind reversibly at the active site so adding more substrate overcomes inhibition, while non-competitive inhibitors bind at an allosteric site causing permanent shape change.

what examiners catch — Students incorrectly state that non-competitive inhibition can be overcome by adding more substrate, or fail to explain that Vmax decreases in non-competitive inhibition but Km stays constant.
what you leave with

four things, not forty.

what's underneath

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this conceptenzyme inhibitionCompetitive inhibitors structurally resemble the substrate and bind reversibly at the active site so adding more substrate overcomes inhibition, while non-competitive inhibitors bind at an allosteric site causing permanent shape change.
sits under itproteins and amino acidsbecause inhibition is done to a protein
the rest of medicinal chemistry

6 more, same treatment.

Each one is its own knowscape in the app — built for how a particular student takes things in, not one explanation handed to everybody.

green chemistry in drug synthesislive →isolation and purificationin the applock and key, and chirality in drugsin the apporganic compounds as medicinesin the apppharmacokinetics and drug designin the appdrug-receptor interactionsin the app
this is one of 865

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