Explain Enzyme Cofactors in Biochemistry Flashcards

A non-protein chemical compound that is bound (either tightly or loosely) to a protein and is required for the protein's biological activity

A cofactor that is tightly bound to a protein. It is permanently attached.

A cofactor that is loosely bound to a protein. It is temporarily attached and detaches after a reaction.

Are molecules that bind to enzymes and decrease their activity.

Bind to enzymes with non-covalent interactions such as hydrogen bonds, hydrophobic interactions and ionic bonds. Multiple weak bonds between the inhibitor and the active site combine to produce strong and specific binding. reversible inhibitors generally do not undergo chemical reactions when bound to the enzyme and can be easily removed by dilution or dialysis.

The substrate and inhibitor compete for access to the enzyme's active site.

The binding of the inhibitor to the enzyme reduces its activity but does not affect the binding of substrate.

Blocks the active site altogether and prevents its functions

Irreversible inhibitors usually covalently modify an enzyme, and inhibition cannot therefore be reversed.