AP BIOLOGY

Detailed explanation-1: -Protein kinases catalyze the transfer of a phosphate moiety from ATP to proteins and phosphatases act to remove this phosphate group by hydrolysis.

Detailed explanation-2: -A phosphatase is an enzyme that removes a phosphate group from a protein. Together, these two families of enzymes act to modulate the activities of the proteins in a cell, often in response to external stimuli.

Detailed explanation-3: -The phosphorylation of a protein can make it active or inactive. Phosphorylation can either activate a protein (orange) or inactivate it (green). Kinase is an enzyme that phosphorylates proteins. Phosphatase is an enzyme that dephosphorylates proteins, effectively undoing the action of kinase.

Detailed explanation-4: -Protein phosphatases Phosphatases have the opposite function of kinases. They remove the phosphate group from phosphoproteins by hydrolyzing phosphoric acid monoesters into a phosphate group and a molecule with a free hydroxyl group (28, 29).

Detailed explanation-5: -Dephosphorylation is the process by which phosphate groups are removed from a molecule by a phosphatase. Removal of phosphate groups from a DNA fragment can prevent ligation. Learn more about dephosphorylation and phosphatases.