Final answer:
The enzyme responsible for the removal of a phosphate group from ATP is called a phosphatase. This enzyme catalyzes dephosphorylation, transforming ATP into ADP and releasing energy for cellular processes.
Step-by-step explanation:
The removal of a phosphate group from ATP is catalyzed by an enzyme known as a phosphatase. This process, called dephosphorylation, occurs when the phosphatase enzyme removes the phosphate group from a molecule that has been previously phosphorylated. The common example of this is when ATP (adenosine triphosphate) is converted into ADP (adenosine diphosphate) and inorganic phosphate (Pi), which also releases energy that can be utilized by the cell for various functions. Conversely, adding a phosphate group to a molecule, such as ADP to form ATP, is referred to as phosphorylation and is typically performed by a different class of enzymes known as kinases.
Importantly, the phosphodiesterase enzyme is responsible for degrading cyclic adenosine monophosphate (cAMP), yielding AMP, which is a way cells terminate signaling pathways. On the other hand, a mutase enzyme, such as phosphoglycerate mutase, is involved in moving a phosphate group within a molecule during glycolysis, which is a different function from removing it altogether.
In summary, phosphatases are key enzymes in cellular metabolism, playing a critical role in reversing the action of kinases and turning off signal transduction pathways by removing phosphate groups from proteins and other molecules.