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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.
What else can I help you with?
What other means does a cell use to control enzymatic activity?
Cells can control enzymatic activity through post-translational modifications such as phosphorylation, allosteric regulation, and feedback inhibition. They can also regulate enzyme synthesis and degradation, as well as by compartmentalizing enzymes in specific organelles or cellular locations.
What mechanism is used to finely tune enzyme activity according to the needs of the cel l?
Allosteric regulation is a mechanism commonly used to finely tune enzyme activity. This involves the binding of a molecule at a site other than the active site, leading to a change in enzyme conformation and subsequent modulation of its activity. By responding to changes in the cellular environment, enzymes can maintain proper levels of activity to meet the cell's metabolic demands.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
Which aspect of lac operon regulation is an example of post-translational control?
The addition of a lactose molecule to the Lac repressor protein is an example of post-translational control in lac operon regulation. This modification prevents the Lac repressor from binding to the operator region, allowing for the transcription of the genes involved in lactose metabolism.
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.
Some enzymatic regulation is allosteric?
yes
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.
What kind of regulation exist for enzymes?
Allosteric regulation and Reversaeble regulation :)
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.
What other means does a cell use to control enzymatic activity?
Cells can control enzymatic activity through post-translational modifications such as phosphorylation, allosteric regulation, and feedback inhibition. They can also regulate enzyme synthesis and degradation, as well as by compartmentalizing enzymes in specific organelles or cellular locations.
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
Does Allosteric regulation depends on inhibitors binding to the active site of enzymes?
No, allosteric regulation involves molecules binding to a site other than the active site (allosteric site) to either activate or inhibit enzyme activity. This type of regulation can involve activators or inhibitors that induce conformational changes in the enzyme, affecting its activity.
What mechanism is used to finely tune enzyme activity according to the needs of the cell?
allosteric regulation
How do allosteric regulation and competitive inhibition differ in their mechanisms of enzyme regulation?
Allosteric regulation involves a molecule binding to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and activity. Competitive inhibition involves a molecule binding to the active site of the enzyme, blocking substrate binding and enzyme activity.
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.
Distinguish between allosteric activation and cooperativity?
cooperativity is an interaction of the subunits of a protein whereby a conformational change in one subunit is transmitted to all others. allosteric regulation is when an activation molecule bonds to an active site where the subunits join.
