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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.
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∙ 9y ago
Wiki User
∙ 16y agoThe allosteric enzymes are the enzymes which in most of the cases are not a part of the process taking place i.e, they are located outside the template where process is occurring and they code for the molecules which have a regulatory influence on the process occurring respectively.
Wiki User
∙ 9y agoAllosteric inhibition refers to the prevention of the pathway by something that binds to the enzyme at a different site then the normal molecule. The shape of the active site is changed during this process.
Wiki User
∙ 14y agoSimply put ' allosteric ' means ' other site. ' In allosteric inhibition generally a allosteric inhibitor inserts itself in to a site other than the active site and deforms the enzyme enough that the active site no longer accepts the substrate. Reversable, course.
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∙ 9y agoyou get insyme
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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.
How can enzyme activity be regulated?
Enzymes are catalytic molecules that speed up the rates of reactions.(a) Explain why enzymes are necessary in biological systems.(b) Discuss three control mechanisms that regulate enzymatic activity.A) Enzymes decrease the amount of activation energy required for chemical reactions to occur.B) 1. Cofactors and Coenzymes- Inorganic ions and non protein organic molecules that are necessary to be present on the active site for some enzymes to work. These cofactors participate in the reaction and may even accept or contribute atoms to the reactions.2. Competitive and Noncompetitive inhibition- Limits the enzyme activity. This occurs when a molecule binds to an enzyme, either on the active site or allosteric site, and decreases its activity.3. Allosteric Regulation- Causes a different shape in the enzyme. May either inhibit or stimulate an enzymes activity.
How is competitive inhibition different from non competitive inhibition?
Competitive Inhibition is a substance that binds to the active site in place of the substance while Non-competitive Inhibition is a substance that binds to a location remote from the active site. (:
What is the type of inhibition of invertase by urea?
Urea is a non-competitive inhibitor which means that the Vmax will decrease and the Km will remain unchanged during the process.
What is inhibition and why enzymes need to be inhibited?
- Inhibition of an enzyme is to inhibit the catalytic activity of the enzyme. - Because, by blocking or inhibiting an enzyme's activity can kill a pathogen or correct a metabolic imbalance. Example : Inhibition of HIV protease.
When a pathway is subject to allosteric feedback inhibition ...?
an accumulation of effectors slows the pathway.
Allosteric inhibition is generally a result of?
binding regulatory molecules at another site
Which type of control agent exerts noncompetitive inhibition?
Protein kinase and Allosteric effector
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
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 are the 3 conditions required for enzymes to do their job properly?
temperature, pH, and allosteric inhibition (at least that's what I said on my bio essay)
What is the general features of allosteric regulation using the feedback inhibition?
enzymes situated at key steps in metabolic pathways are modulated by allosteric effectors these effectors are usually produced elsewhere in the pathway effectors may be feed-forward activators or feedback inhibitors kinetics are sigmoid ("S-shaped")
How do most cells regulate the activity of enzymes?
Enzyme speeds up the chemical reaction. So, it would speed the cells for life and live.
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 happens to an allosteric enzyme when the concentration of substrate around the?
B. it increases its processin capacity
Why does adding additional substrate overcome competitive but not noncompetitive inhibition?
A competitive inhibitor competes with the substrate to bind to the active site while a noncompetitive inhibitor binds to an allosteric site of the enzyme (one other than the active site). Thus no amount of substrate can overcome or in a sense interfere with the inhibitors binding to an allosteric site.
Diffusion of nonpolar molecules would not be affected by?
Diffusion of nonpolar molecules would not be affected by charge. Allosteric inhibition is generally a result of binding regulatory molecule at a site other than the active site.
