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Yes, the allosteric effect can change an enzyme's function by altering its activity or affinity for its substrate. This modulation is often achieved by a molecule binding to a site on the enzyme other than the active site, causing a conformational change that affects the enzyme's catalytic activity.
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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 are the two environmental factors that effect the function of enzymes?
tempeture,ph, solute concentration and salt content
What can effect how the enzyme and substrate come together?
Factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators can affect how enzymes and substrates come together. Changes in these factors can alter the shape and activity of enzymes, impacting their ability to bind with substrates and catalyze reactions.
What is found in allosteric enzymatic regulation?
Allosteric enzymatic regulation involves the binding of a molecule at a site other than the active site, leading to a change in enzyme activity. This regulation can enhance or inhibit enzyme activity, depending on the nature of the allosteric molecule and its binding effects.
Why will increasing the substrate concentration not decrease the effect of a non competitive inhibitor?
Increasing the substrate concentration will not decrease the effect of a noncompetitive inhibitor because a noncompetitive inhibitor binds to an allosteric site on the enzyme, which is different from the active site where the substrate binds. Therefore, increasing the substrate concentration does not compete with the noncompetitive inhibitor for binding.
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 are the two environmental factors that effect the function of enzymes?
tempeture,ph, solute concentration and salt content
What can effect how the enzyme and substrate come together?
Factors such as temperature, pH, substrate concentration, and the presence of inhibitors or activators can affect how enzymes and substrates come together. Changes in these factors can alter the shape and activity of enzymes, impacting their ability to bind with substrates and catalyze reactions.
How is it possible for a point mutation to have no effect on the function of gene?
If the point mutation does not change the protein to be translated in the 3-letter sequence, then it will have no effect on the gene's function.
What is found in allosteric enzymatic regulation?
Allosteric enzymatic regulation involves the binding of a molecule at a site other than the active site, leading to a change in enzyme activity. This regulation can enhance or inhibit enzyme activity, depending on the nature of the allosteric molecule and its binding effects.
How does pH effect how enzymes function?
pH can affect the function of enzymes by altering the charge on the amino acid residues in the enzyme's active site. Subtle changes in pH can disrupt the hydrogen bonding and electrostatic interactions that are necessary for enzyme-substrate binding and catalysis. Extreme pH values can denature enzymes, resulting in loss of their structure and consequently their function.
What effect does enzymes have on the cholesterol?
It has no effect
What effect does flash pasteurization have on the proteolytic enzymes and the digestive enzymes?
not a thing
PH effect on enzymes?
pH can significantly affect the function of enzymes by altering their shape and charge, ultimately impacting their ability to bind substrates and catalyze reactions. Each enzyme has an optimal pH at which it works most efficiently, and deviations from this pH can lead to reduced activity or denaturation of the enzyme. It is important to maintain an appropriate pH for enzymes to function properly in biological systems.
How do allosteric regulation and competitive inhibition compare?
Allosteric regulation involves a regulator molecule binding to a site other than the active site to change enzyme activity. Competitive inhibition involves a molecule blocking the active site to prevent substrate binding. Both can regulate enzyme activity, but allosteric regulation is noncompetitive and can have either an activating or inhibitory effect, whereas competitive inhibition only inhibits enzyme activity.
Why will increasing the substrate concentration not decrease the effect of a non competitive inhibitor?
Increasing the substrate concentration will not decrease the effect of a noncompetitive inhibitor because a noncompetitive inhibitor binds to an allosteric site on the enzyme, which is different from the active site where the substrate binds. Therefore, increasing the substrate concentration does not compete with the noncompetitive inhibitor for binding.
What effect has pH on enzymes?
pH influences enzyme activity by affecting the shape and charge of the active site. Most enzymes have an optimum pH at which they function most effectively. Deviating from this pH can denature the enzyme and reduce its activity.
