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What is the difference between an allosteric enzyme and a non-allosteric enzyme?
Wiki User
∙ 10y ago
alloesterinc enzymes have 2 or more binding sites which can bind the same or different molecules. When a molecule bind one of the sites the other site changes conformation and gets a higher affinity for a ligand. this is allostric coorporation. alloestric sites can also regulate binding of a ligand by preventing binding if they are occupied. this is alloesteric regulation. allo means "other" sterio means "site" so allosteric means "other site". a regular enzyme has one or more binding sites but they are independent of each other i.e. binding of a ligand to one site does not increase or decrease affinity of binding in the other site.
Wiki User
∙ 10y ago
Wiki User
∙ 11y agoAllosteric activator has two or more subunits and allosteric has one
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What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
An allosteric inhibitor stops enzyme activity by binding to an allosteric site and causing the conformation of the enzyme to change.
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 phosphofructokinase?
Phosphofructokinase (PFK) is an enzyme that generates energy from carbohydrates during physical activity.
Phosphofructokinase is an important control enzyme in the regulation of cellular respiration of cellular respiration What is statement that describes a function of phosphofructokinase?
it is an allosteric enzyme.
What would be unlikely to contribute to the substrate specificity of an enzyme?
The allosteric site is distinct from the active site, and does not affect the substrate specificity of the enzyme
What blocks enzyme activity by binding to allosteric site of an enzyme causing the enzyme's active site to change shape?
An allosteric inhibitor stops enzyme activity by binding to an allosteric site and causing the conformation of the enzyme to change.
What is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
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 statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
Does the allosteric effect in an enzyme change the enzyme's function?
allosteric effectors have their own specific sites for binding to enzyme. they can bring positiveor negative effect. that depends on the natre of effector.
An allosteric enzyme made up of protein subunits alternates between active and inactive forms?
true
What is Difference between uncompetitive and non competitive enzyme inhibition?
I believe non competitive antagonists bind to an allosteric site that prevents the enzyme from binding substrate whereas uncompetitive binds and stabilizes the ES complex which slows down the reaction.
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 "
What is found in allosteric enzymatic regulation?
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.
True or false an allosteric enzyme made up of protein subunits alternates between active and inactive forms?
true
What can effect how the enzyme and substrate come together?
Shape of substrate, shape of the enzyme, Competitive, noncompetitive and allosteric inhibitors.
What is phosphofructokinase?
Phosphofructokinase (PFK) is an enzyme that generates energy from carbohydrates during physical activity.
