Enzyme Inhibition Types Quiz

A process that regulates enzyme activity by decreasing or stopping its function.

A substance that decreases or abolishes the rate of enzyme action.

Enzyme inhibition where the inhibitor structurally resembles the substrate and competes for the same active site.

Enzyme inhibition where the inhibitor doesn't resemble the substrate and binds to a different site on the enzyme.

Competitive inhibition is reversible, meaning it can be overcome by increasing the concentration of the substrate.

Non-competitive inhibition is irreversible, meaning it cannot be overcome by increasing the concentration of the substrate.

A measure of the enzyme's affinity for its substrate. Lower Km means higher affinity.

The maximum rate of an enzyme-catalyzed reaction.

In competitive inhibition, Vmax remains unchanged, but Km increases.

In non-competitive inhibition, Vmax decreases, but Km remains unchanged.

The formation of a complex between the enzyme and the inhibitor (EI).

The formation of a complex between the enzyme, substrate, and inhibitor (ESI).

A type of non-competitive inhibition where the inhibitor binds to the enzyme's active site and prevents it from binding to its substrate.

A type of non-competitive inhibition where the inhibitor binds to a site other than the active site and alters the enzyme's shape, thus preventing it from binding to its substrate.

A drug that inhibits the enzyme dihydropteroate synthase, involved in folic acid synthesis in bacteria.

A drug that inhibits the enzyme vitamin K epoxide reductase, involved in prothrombin synthesis.

A drug that inhibits the enzyme xanthine oxidase, involved in the conversion of xanthine to uric acid.

A type of non-competitive inhibition that involves the inhibition of the sulfhydryl (-SH) group, crucial for enzyme activity.

A type of non-competitive inhibition where the inhibitor targets cofactors, molecules essential for enzyme activity.

A type of non-competitive inhibition where the inhibitor targets specific metal ions that act as activators for enzymes.

Heavy metals, such as mercury (Hg++) and lead (Pb++), can inhibit enzymes by blocking their sulfhydryl (-SH) groups.

A coenzyme involved in reactions like transamination, decarboxylation, and deamination.

Cyanide and hydrazine inhibit the action of PLP, often by binding to it and preventing its function.

Carbon monoxide (CO) and cyanide inhibit cytochrome oxidase by blocking the iron in the heme, a critical prosthetic group.

Oxalate can prevent blood clotting by chelating calcium ions, which are essential for the activation of thrombokinase.

Fluoride can inhibit glycolysis by chelating magnesium ions, which are crucial for the activity of enolase.

A condition caused by the accumulation of sodium urate crystals in joints and joint fluid, leading to pain and inflammation.

Ischemic heart disease is a condition caused by reduced blood flow to the heart, often due to narrowed arteries.

The buildup of uric acid, a waste product of purine metabolism.