Does anyone know what the difference is between an allosteric enzyme and a enzyme that is not allosteric?
yes, I do. =)
okay, JK. an allosteric enzyme is an enzyme that can be inhibited by an allosteric effector. this is a molecule that binds to a binding site off the reactive site and induces a conformation change in the enzyme, thus inhibiting it. non-allosteric enzymes can not be effected by allosteric inhibitors. but they are, as all enzymes, vulnerable to cometitive inhibitors.
Thanks.
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So allosteric enzymes, can be turned on and off by the attatchment of a ligand?
yes. but the important thing is that this ligand doesn't bind where the substrate binds, but somewhere else on the enzyme ("action at a distance"). non-allosteric enzymes can also be turned off, but by ligands blocking the reaction site (which is the same place as the substrate woul bind).
Is the enzyme isocitrate dehydrogenase inactivated by NADH, in citric acid cylcle?
Is it an example of how allosteric enzymes are the place where the products of the cylcle are regulated?
Allosteric enzymes are proteins that can be binded by small molecules other than the active site that changes their activity [activator/inhibitor]. This can be seen by looking at an activity vs substrate graph. It would have a sigmoidal curve. Examples of allosteric enzymes are PFK1 and ATC [Aspartate Transcarbamoylase]. Both of these enzymes can be activated or inhibited. Inhibited doesnt mean it stops working [inactive] but it takes more substrate to redeem normal activity. [Credential: Currently taking Biochemistry 651.... Currently have an A in the class..... My final is in 3 days.]
Allosteric enzyme activity can be regulated. Normal enzymes act as ON or OFF (means 100% activity OR no activity at all) while allosteric enzyme can act at different rate (10% or any other). It is governed by binding of molecule to site which is other than active site.
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