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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.

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14y ago
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11y ago

In feedback inhibition, the allosteric effect lowers the affinity of the enzyme for its substrate.

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10y ago

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.

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13y ago

an enzyme with more than one subunit

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Q: What is found in allosteric enzymatic regulation?
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Related questions

Some enzymatic regulation is allosteric?

yes


Some enzymatic regulation is allosteric In such cases which of the following would usually be found?

an enzyme with more than one subunit, not feedback inhibition.


What kind of regulation exist for enzymes?

Allosteric regulation and Reversaeble regulation :)


Which aspect of lac operon regulation is an example of post-translational control?

allosteric regulation of CAP


Certain key molecules can regulate biochemical pathways by controlling the rate of enzymatic reactions by binding at?

allosteric sites


What is Role of allosteric enzyme in regulation of purine synthesis?

if the purine synthesis is excess then extra product will bind to the allosteric site then feed back inhibition occurs


True or False 'A change in the primary sequence of a protein can affect allosteric regulation'?

true


Draw a diagram to show how allosteric regulation can be used to regulate biochemical pathways?

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.


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 mechanism is used to finely tune enzyme activity according to the needs of the cell?

allosteric regulation


What mechanism is used to finely tune enzyme activity according to the needs of the cel l?

allosteric regulation


Does Allosteric regulation depends on inhibitors binding to the active site of enzymes?

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.