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A change in the rate of enzyme action in aquatic invertebrates would most directly result from a change in what?

A change in the rate of enzyme action in aquatic invertebrates would most directly result from a change in temperature, pH, or substrate availability in their environment. These factors can influence the activity and efficiency of enzymes in these organisms.


Which enzyme shows the greatest change in its rate of action with the least change in pH?

The enzyme pepsin shows the greatest change in its rate of action with the least change in pH. Pepsin works optimally at a highly acidic pH of around 2, and even small changes in pH can significantly impact its activity.


What change would not affect the relative rate of action of enzyme x?

increase of temp in 70- 80 degrees


How does increasing enzyme concentration affect the rate of enzyme action when the enzyme concentration remains constant?

It doesn't


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.


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.


What kinds of chemicals might you add to try to speed up the action of an enzyme or to inhibit its action?

To speed up the action of an enzyme, you can add cofactors or coenzymes that are required for the enzyme's activity. Inhibitors can be used to block or reduce the enzyme's activity, such as competitive inhibitors that compete with the substrate for the active site, or non-competitive inhibitors that bind to another part of the enzyme and alter its shape.


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.


How does noncompetitive inhibition differ from allosteric inhibition in terms of their mechanisms of action on enzyme activity?

Noncompetitive inhibition and allosteric inhibition both affect enzyme activity, but through different mechanisms. Noncompetitive inhibition 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. Allosteric inhibition, on the other hand, binds to a different site on the enzyme called the allosteric site, which also causes a change in the enzyme's shape and reduces its activity.


Why does pH affect enzyme action?

yeh it can


What are anti enzymes?

Anti enzymes or enzyme inhibitors, are substances which inhibit counteracts the action of an enzyme.