Final answer:
Phosphorylation is the process by which enzymes transfer a terminal phosphate group from ATP to another molecule, often mediated by kinases, as exemplified by glycolytic enzymes like phosphoglycerate kinase and pyruvate kinase.
Step-by-step explanation:
Phosphorylation in Biological Systems
When enzymes transfer the terminal phosphate group from ATP to another molecule, this process is known as phosphorylation. This critical reaction occurs in various metabolic pathways and is fundamental in cellular energy transfer. In a typical phosphorylation reaction, ATP binds to the enzyme and another substrate in the reaction to form an intermediate complex, facilitating the transfer of the phosphate group to the substrate. In essence, the energy carried by this phosphate group is used to modify the substrate and convert it into another product. Enzymes like kinases play a pivotal role in these reactions through substrate-level phosphorylation.
An example of this process is during glycolysis where phosphoglycerate kinase catalyzes the substrate-level phosphorylation, transferring a phosphate from 1,3-bisphosphoglycerate to ADP to form ATP. The transformation of glucose into glucose phosphate (C6H12O6-P) upon entering a cell is another instance of phosphorylation, which enables glucose to be stored as glycogen or metabolized. Similarly, pyruvate kinase catalyzes the transfer of a phosphate from phosphoenolpyruvate (PEP) to ADP, forming ATP, and a molecule of pyruvate, demonstrating another high-energy phosphate transfer.