Final answer:
An enzyme that phosphorylates a substrate is called a kinase. Phosphorylation involves adding a phosphate group to a substrate, a reaction catalyzed by enzymes such as phosphoglycerate kinase. Phosphatases remove phosphate groups, thereby dephosphorylating substrates, which is the opposite of what kinases do.
Step-by-step explanation:
No, the enzyme that modifies a substrate by phosphorylating it is called a kinase, not phosphatase. A phosphatase is an enzyme that performs the opposite function, which is to remove a phosphate group from a substrate, a process known as dephosphorylation.
In biology, specific enzymes are responsible for transferring phosphate groups to various substrates. This process is called phosphorylation. For example, the enzyme phosphoglycerate kinase catalyzes the transfer of a high-energy phosphate from 1,3-bisphosphoglycerate to ADP, producing ATP. This reaction is a form of substrate-level phosphorylation and is crucial in metabolic pathways like glycolysis. Kinases, such as phosphoglycerate kinase, are responsible for this transfer and are widely recognized for their role in signaling pathways and cellular regulation.
Conversely, phosphatases remove phosphate groups, reversing the action of kinases. Removing the phosphate group often results in a change in the structure and function of the substrate. This mechanism is a way for the cell to control enzyme activity and regulate metabolic pathways. Therefore, phosphorylation and dephosphorylation act as on/off switches in many cellular processes.