ophosphorylation
Phosphorylation is a post-translational modification in which a phosphate group is covalently attached to a protein or other organic molecule. This process is primarily catalyzed by enzymes known as kinases, which transfer the phosphate group from a donor molecule, typically adenosine triphosphate (ATP), to a specific amino acid residue on the target protein. The most common sites for phosphorylation are serine, threonine, and tyrosine residues, although other amino acids such as histidine, asparagine, and cysteine can also be phosphorylated under certain conditions.
Phosphorylation plays a critical role in regulating various cellular processes, including signal transduction, enzyme activity, protein-protein
The reverse process, dephosphorylation, is mediated by enzymes called phosphatases, which remove phosphate groups from proteins.
Phosphorylation can also influence protein localization, stability, and interactions with other molecules. For instance, phosphorylation may