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When a product binds to an allosteric enzyme to slow its reaction what does it do?
When a product binds to an allosteric enzyme to slow its reaction, it is acting as a negative allosteric regulator. This binding causes a conformational change in the enzyme, reducing its affinity for the substrate and slowing down the overall reaction rate.
Some enzymatic regulation is allosteric In such cases which of the following would usually be found?
In allosteric enzyme regulation, the regulator molecule binds to a site other than the active site, called the allosteric site. This binding alters the enzyme's activity by inducing a conformational change in the enzyme structure. This can either activate or inhibit the enzyme's function, depending on the nature of the allosteric regulator.
How do allosteric regulation and competitive inhibition compare?
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.
What is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
Is allosteric inhibition competitive or noncompetitive?
Allosteric inhibition is a type of noncompetitive inhibition.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
How allosteric enzymes differ non allosteric?
Allosteric enzymes have an additional regulatory site (allosteric site) distinct from the active site that can bind to specific molecules, affecting enzyme activity. Non-allosteric enzymes lack this additional regulatory site and their activity is primarily controlled by substrate binding to the active site. Allosteric enzymes show sigmoidal kinetics in response to substrate concentration due to cooperativity, while non-allosteric enzymes exhibit hyperbolic kinetics.
What is the allosteric inhibitor?
The inhibitor which binds or attached with the allosteric site of enzyme k/n as A.I ... BY "NAHEED KHATTI "
Is uncompetitive inhibition an example of allosteric regulation in enzyme activity?
Yes, uncompetitive inhibition is an example of allosteric regulation in enzyme activity.
True or False 'A change in the primary sequence of a protein can affect allosteric regulation'?
True. A change in the primary sequence of a protein can alter its three-dimensional structure, which in turn can affect the binding of allosteric regulators and thus impact allosteric regulation.
Some enzymatic regulation is allosteric?
yes
What is allosteric inhibitor of glutamate dehydrogenase?
GTP
