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How malonate inhibit the conversion of succinate to fumarate?
Malonate is a competitive inhibitor of succinate dehydrogenase, the enzyme responsible for converting succinate to fumarate in the citric acid cycle. Malonate resembles succinate and competes for the active site of succinate dehydrogenase. As a result, malonate binds to the enzyme and prevents succinate from binding, inhibiting the conversion of succinate to fumarate.
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.
How would one overcome the effects of a competitive inhibitor on enzyme activity in the biochemical regulation of metabolic pathways?
One way to overcome the effects of a competitive inhibitor on enzyme activity is to increase the substrate concentration. By increasing the substrate concentration, you can outcompete the inhibitor for binding to the enzyme's active site. Another strategy is to use allosteric regulators that can bind to a separate site on the enzyme and change its conformation, potentially reducing the inhibitor's binding affinity.
What statement best describes the function of a competitive inhibitor in an enzyme-catalyzed reaction?
Competitive inhibitor is a substance that competes directly with a normal substrate for an enzymatic-binding site of an enzyme. Such an inhibitor usually resembles the substrate to the extent that it specifically binds to the active site of the enzyme but differs from it so as to be unreactive and therefore there will be no catalytic reaction. Some examples are: methotrexate that is competitive inhibitor of dihydrofolate reductase, and malonate which structurally resembles succinate (that is converted to fumarate by succinate dehydrogenase during the citric acid cycle) but cannot be dehydrogenated.
What statement is characteristic of allosteric effectors?
Allosteric effectors may not resemble the enzyme's substrates.
Which one of the following would you predict is an allosteric inhibitor of the Krebs cycle enzyme ketoglutarate dehydrogenase?
It is likely that ATP could act as an allosteric inhibitor of ketoglutarate dehydrogenase in the Krebs cycle. High levels of ATP signal that the cell has sufficient energy, so it would make sense for ATP to inhibit an enzyme involved in generating more energy through the cycle.
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 "
Why glutamate dehydrogenase synthesised only in liver?
Glutamate dehydrogenase is only synthesized in the liver because it would be toxic elsewhere in the body.
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.
What is the difference between a competitive inhibitor and an allosteric inhibitor in terms of their mechanisms of action on enzymes?
A competitive inhibitor competes with the substrate for the active site of an enzyme, blocking its function. An allosteric inhibitor binds to a different site on the enzyme, causing a conformational change that reduces the enzyme's activity.
What is Malonic acids role with respect to succinate dehydrogenase?
Malonic acid is a competitive inhibitor of succinate dehydrogenase.
Which enzyme catalyzes glutamate oxidative deamination?
Glutamate dehydrogenase an mitochondrial enzyme helps in oxidative deamination of glutamate It helps to take out the ammonium group from glutamate to make it available for urea synthesis
What is the difference between an allosteric inhibitor and a competitive inhibitor in terms of their mechanisms of action on enzyme activity?
An allosteric inhibitor binds to a site on the enzyme that is separate from the active site, causing a change in the enzyme's shape and reducing its activity. A competitive inhibitor, on the other hand, competes with the substrate for binding to the active site of the enzyme, blocking its function.
How does an allosteric inhibitor function to regulate enzyme activity?
An allosteric inhibitor regulates enzyme activity by binding to a site on the enzyme that is different from the active site. This binding changes the enzyme's shape, making it less effective at catalyzing reactions.
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.
Which type of control agent exerts noncompetitive inhibition?
A noncompetitive inhibitor binds to an allosteric site on the enzyme, causing a conformational change that reduces the enzyme's activity without competing with the substrate for the active site. This type of control agent is called a noncompetitive inhibitor.
What has the author Michael Graham Gore written?
Michael Graham Gore has written: 'Studies on the glutamate dehydrogenase of Neurospora crassa'
