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The inhibitor which binds or attached with the allosteric site of enzyme k/n as A.I ... BY "NAHEED KHATTI "
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What is allosteric inhibitor of glutamate dehydrogenase?
GTP
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.
Which one of the following would you predict is an allosteric inhibitor of the Krebs cycle enzyme ketoglutarate dehydrogenase?
NADH
What is an inhibitor that forms a covalent bond with an amino acid side group within the active site?
Competitive inhibitor source - AP Bio Text Book
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.
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.
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 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 characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
How allosteric enzymes differ non allosteric?
Allosteric enzymes have the ability to change their conformational ensemble after binding. This changes their affinity at a different ligand binding site.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
What are the two different types of inhibition?
Increasing the temperature excessively - if an enzyme is heated too much (usually around 40°C) the enzyme will become denatured. This will prevent it from working permanently. Decreasing the temperature - decreases enzyme activity Enzyme inhibitors - heavy metals poison enzymes by binding to the active site, preventing the enzyme from binding to the substrate molecule.
