An allosteric enzyme is one in which the activity of the enzyme can be controlled by the biniding of a molecule to the "allosteric site". This really just means somewhere other than the active site. Thus allosteric control of an enzyme can be classed in two ways. A positive allosteric modification is the binding of a molecule to the enzyme which increase the rate of reaction. Sort of like catalysing the catalysing effect of an enzyme. Obviously the opposite is true of negative allosteric modification. A good example for this is the activity of phosphofructokinase, which is promoted by a high AMP concentration, and inhibited by a high ATP concentration. This should make sense if you think about the action of a kinase etc.
In feedback inhibition, the allosteric effect lowers the affinity of the enzyme for its substrate.
The active site becomes available to the substrate when regulatory molecules binds to diffirent site of your enzyme or vice versa, you are the controller.
an enzyme with more than one subunit
allosteric regulation of CAP
allosteric regulation
The area where a molecule other than substrate can attach is called the allosteric site.
enzymes situated at key steps in metabolic pathways are modulated by allosteric effectors these effectors are usually produced elsewhere in the pathway effectors may be feed-forward activators or feedback inhibitors kinetics are sigmoid ("S-shaped")
Allosteric enzymes have the ability to change their conformational ensemble after binding. This changes their affinity at a different ligand binding site.
yes
an enzyme with more than one subunit, not feedback inhibition.
Allosteric regulation and Reversaeble regulation :)
allosteric regulation of CAP
allosteric sites
if the purine synthesis is excess then extra product will bind to the allosteric site then feed back inhibition occurs
true
A diagram cannot be drawn to answer this question. An answer to how allosteric regulation can be used to regulate biochemical pathways needs to be written or spoken. This question cannot be answered in its current form.
A competitive inhibition and allosteric regulation both involves an inhibitor molecule binding to the enzyme at a different area. The difference between the two is that allosteric inhibitors are modulator molecules which bind somewhere besides the catalytic activity.
allosteric regulation
allosteric regulation
Of course. That is the meaning of ' noncompetitive inhibitor. ' It does not compete with the substrate at the active site but inhibits enzyme activity at the allosteric ( other site ) site.