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What is the place where the substrate attaches to the enzyme?
The active site is where the substrate binds to the enzyme. It is a region on the enzyme where the chemical reaction takes place. The active site is specific to the substrate molecule, allowing for precise catalysis to occur.
How At high temperatures the rate of enzyme action decreases because the increased heat?
alters the active site of the enzyme
What happen to the active site when the enzyme denatures?
The action going on that site will slow down.
Does temperature change the active site of an enzyme?
Yes, temperature can affect the active site of an enzyme. Low temperatures can slow down enzyme activity by reducing molecular motion and interactions, while high temperatures can denature the enzyme by disrupting its structure and causing it to lose its function. Each enzyme has an optimal temperature at which it functions best.
Although trypsin is a proteolytic enzyme it does not digest the tissue in which it is produced?
Trypsin is produced in the Duodenum . The enzyme trypsin is a serine protease which is active at a pH of 8 and at a temp optima of 37 degrees. The pH of the duodenum is around 6-6.5 which is not enough for the kinetic activation of the enzyme. Hence it is inactive in its production site wheras the condition is just optimum for its action in the pancreas.
How does allosteric inhibition differ from noncompetitive inhibition in terms of their mechanisms of action on enzyme activity?
Allosteric inhibition occurs when a molecule binds to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, but it does not change the enzyme's shape. This type of inhibition reduces the enzyme's activity by blocking the active site or altering the enzyme's ability to bind to the substrate.
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.
At high temperatures the rate of enzyme action decreases because the increased heat?
alters the active site of the enzyme
What is the site of action for trypsin?
Enzyme trypsin is one of the enzymes that plays part during the process of digestion. Its site of action is in the small intestine where it breaks protein to large peptides.
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 do noncompetitive and allosteric inhibitors differ in their mechanisms of action on enzymes?
Noncompetitive inhibitors bind to a site on the enzyme that is not the active site, causing a change in the enzyme's shape and preventing substrate binding. Allosteric inhibitors bind to a different site on the enzyme, causing a conformational change that affects the active site's ability to bind substrate.
How do allosteric inhibition and noncompetitive inhibition differ in their mechanisms of action on enzymes?
Allosteric inhibition occurs when a molecule binds to a site on an enzyme that is not the active site, causing a change in the enzyme's shape and reducing its activity. Noncompetitive inhibition, on the other hand, involves a molecule binding to the enzyme at a site other than the active site, which does not change the enzyme's shape but still reduces its activity.
