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An enzyme inhibitor are compounds that are built to block enzymes. These inhibitors blocks enzymes in such a way that the enzymes are prevented on doing whatever task it's meant to do.

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How do you use inhibitor in a sentence?

An enzyme inhibitor is a substance that binds to an enzyme and decreases the enzyme's activity.


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.


Where does an uncompetitive inhibitor bind in relation to the enzyme-substrate complex?

An uncompetitive inhibitor binds to the enzyme-substrate complex after the substrate has already bound to the enzyme.


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.


Where does a noncompetitive inhibitor bind in relation to the enzyme's active site?

A noncompetitive inhibitor binds to a site on the enzyme that is not the active site.


Which blocks enzyme activity by binding to the site of an enzyme?

inhibitor


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 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.


What happens to the vmax when a competitive reversible inhibitor is added to an enzyme?

The Vmax of the enzyme will remain constant in the presence of a competitive reversible inhibitor. However, the apparent Km will increase as the inhibitor competes with the substrate for binding to the active site of the enzyme, leading to a decrease in enzyme-substrate affinity.


Blocks the action of the enzyme that causes the blood vessels to contract resulting in hypertension?

ACE inhibitor


How does a noncompetitive enzyme inhibitor function to inhibit enzyme activity?

A noncompetitive enzyme inhibitor works by binding to the enzyme at a site other than the active site, causing a change in the enzyme's shape. This change makes it harder for the substrate to bind to the enzyme, reducing its activity.


What is the impact of an uncompetitive inhibitor on the values of Km and Vmax in enzyme kinetics?

An uncompetitive inhibitor decreases both the Km and Vmax values in enzyme kinetics.