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What is allosteric activator?
An allosteric activator is a molecule that binds to a specific site on an enzyme, distinct from the active site, and enhances the enzyme's activity. This binding induces a conformational change in the enzyme, leading to an increase in its catalytic activity. Allosteric activators are essential for regulating enzyme activity in various cellular processes.
In an allosteric enzyme the homotropic effect is seen when?
In an allosteric enzyme, the homotropic effect occurs when the substrate acts as a ligand and binds to the active site, influencing the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, depending on the specific enzyme and substrate involved.
What binds to the enzyme and plays a role in catalyst?
A substrate binds to the enzyme and plays a role in catalysis by undergoing a chemical reaction with the enzyme. This interaction allows the enzyme to convert the substrate into a product, usually by lowering the activation energy required for the reaction to occur. Additionally, cofactors or coenzymes may also bind to the enzyme to assist in catalysis by providing or accepting functional groups during the reaction.
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.
When allosteric effector X binds to enzyme the enzyme stops working. Nevertheless the speed of the reaction can be altered by adjusting the concentration of X. How?
If the amount is less, it will take time for the effector to bind to each site. If it is more, it will take less time for the effort to bind. It is like some little kids trying to find a place to sit on a bus. The more there are of them, the faster the seats will be filled.
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 the difference between a noncompetitive inhibitor and an allosteric inhibitor in enzyme regulation?
A noncompetitive inhibitor binds to an enzyme at a site other than the active site, while an allosteric inhibitor binds to a different site on the enzyme, causing a change in the enzyme's shape and reducing its activity.
How does noncompetitive inhibition differ from allosteric inhibition in terms of their mechanisms of action on enzyme activity?
Noncompetitive inhibition and allosteric inhibition both affect enzyme activity, but through different mechanisms. Noncompetitive inhibition binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Allosteric inhibition, on the other hand, binds to a different site on the enzyme called the allosteric site, which also causes a change in the enzyme's shape and reduces its activity.
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 allosteric activator?
An allosteric activator is a molecule that binds to a specific site on an enzyme, distinct from the active site, and enhances the enzyme's activity. This binding induces a conformational change in the enzyme, leading to an increase in its catalytic activity. Allosteric activators are essential for regulating enzyme activity in various cellular processes.
In an allosteric enzyme the homotropic effect is seen when?
In an allosteric enzyme, the homotropic effect occurs when the substrate acts as a ligand and binds to the active site, influencing the enzyme's activity. This binding can either enhance or inhibit the enzyme's function, depending on the specific enzyme and substrate involved.
An enzyme whose activity is affected when a molecule binds to a certain site other than the active site is called?
an allosteric enzyme
What is the difference between an allosteric inhibitor and a noncompetitive inhibitor in terms of their mechanisms of action on enzyme activity?
An allosteric inhibitor binds to a site on the enzyme that is different from the active site, causing a change in the enzyme's shape and reducing its activity. A noncompetitive inhibitor binds to either the enzyme or the enzyme-substrate complex, also reducing enzyme activity but without directly competing with the substrate for the active site.
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.
In a chemical reaction a reactant binds to an enzyme at a region known as the?
active site. This is where the reaction takes place and the substrate interacts with the enzyme to form the product. The active site has a specific shape that fits the substrate, allowing for the reaction to occur.
What happens during allosteric inhibition?
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.
How does allosteric inhibition differ from competitive inhibition in terms of their mechanisms of action on enzymes?
Allosteric inhibition and competitive inhibition are two ways enzymes can be regulated. Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Competitive inhibition, on the other hand, occurs when a molecule binds to the active site of the enzyme, blocking the substrate from binding and inhibiting the enzyme's activity. In summary, allosteric inhibition affects enzyme activity by binding to a site other than the active site, while competitive inhibition affects enzyme activity by binding to the active site directly.
