What do enzymes require for activation from their zymogen form?

Enzymes in their zymogen form are inactive precursors that require specific modifications for activation. The correct answer involves the hydrolysis of the zymogen. This process typically involves the cleavage of specific peptide bonds within the zymogen structure, which results in a conformational change that activates the enzyme.

The activation by hydrolysis is a crucial regulatory mechanism in enzymology, ensuring that the enzyme is only active when required, thereby preventing unwanted reactions in the cell. For instance, digestive enzymes like trypsin are synthesized as zymogens (e.g., trypsinogen) and are activated in the small intestine through the action of proteases that cleave the zymogen.

While other processes like increasing temperature or the transfer of phosphate groups can affect enzyme activity, they do not specifically activate the zymogen form. Covalent attachments of cofactors can also play a role in enzyme function but are not necessary for the conversion of a zymogen to its active form.