Final answer:
Enzymes can be activated by the addition of a phosphate group through phosphorylation, which is catalyzed by a kinase, and deactivated by phosphatases removing the phosphate group.
Step-by-step explanation:
Some target enzymes are activated by the addition of a phosphate group (phosphorylation) by a kinase, and inactivation is catalyzed by a phosphatase.
Phosphorylation is a process where a phosphate group is added to molecules like proteins, often to serine, threonine, or tyrosine residues. This chemical modification is essential in cell signaling pathways, affecting enzyme activity or interaction with other molecules in the signaling cascade.
A kinase catalyzes the transfer of a phosphate group from a donor molecule (usually ATP) to an acceptor molecule, such as a protein, typically triggering a functional change in the target molecule, like enzyme activation. Conversely, phosphatases remove these phosphate groups, reversing the modifications and often resulting in the inactivation of the enzyme or other molecule.