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Allosteric enzymes have the ability to change their conformational ensemble after binding. This changes their affinity at a different ligand binding site.
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What can prohibit enzymes from working in the body?
the various inhibitory molecules such as allosteric inhibitors, poisons, other ihhibitory molecules
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")
One way in which inorganic catalysts and enzymes differ is?
Enzymes are temperature-sensitive, inorganic catalysts are not.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
What causes the enzymes active site to change shape?
When too much of a certain compound is made, the compound attaches to a separate site called allosteric site. When attached to the allosteric site, it changes the active site's shape and prevents any more to be made.
Allosteric enzymes are most effective when the substrate concentration is?
d
What kind of regulation exist for enzymes?
Allosteric regulation and Reversaeble regulation :)
What can prohibit enzymes from working in the body?
the various inhibitory molecules such as allosteric inhibitors, poisons, other ihhibitory molecules
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.
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.
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 functions do allosteric enzymes serve in reaction sequences?
Enzyme reaction rates can be decreased by various types of enzyme inhibitors. ... Enzymes serve a wide variety of functions inside living organisms
How enzymes differ from toxins?
Their spelling
What is the difference between an allosteric enzyme and a non-allosteric enzyme?
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.
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")
One way in which inorganic catalysts and enzymes differ is?
Enzymes are temperature-sensitive, inorganic catalysts are not.
What is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
