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 effectors may not resemble the enzyme's substrates.
Allosteric enzymes have the ability to change their conformational ensemble after binding. This changes their affinity at a different ligand binding site.
Allosteric effectors may not resemble the enzyme's substrates.
The inhibitor which binds or attached with the allosteric site of enzyme k/n as A.I ... BY "NAHEED KHATTI "
An allosteric inhibitor stops enzyme activity by binding to an allosteric site and causing the conformation of the enzyme to change.
yes
GTP
Allosteric (noncompetitive) inhibition results from a change in the shape of the active site when an inhibitor binds to an allosteric site. When this occurs the substrate cannot bind to its active site due to the fact that the active site has changed shape and the substrate no longer fits. Allosteric activation results when the binding of an activator molecule to an allosteric site causes a change in the active site that makes it capable of binding substrate.
if the purine synthesis is excess then extra product will bind to the allosteric site then feed back inhibition occurs
allosteric effectors have their own specific sites for binding to enzyme. they can bring positiveor negative effect. that depends on the natre of effector.
d