Phosphorylation is one of the most prevalent and frequently studied post-translational modification (PTM). Protein phosphorylation is a PTM that plays a key role in regulating signal transduction, apoptosis, and cell cycle and replication. Despite its prevalence, phosphorylation occurs only on three amino acids: Serine (Ser; S), Threonine (Thr; T) and Tyrosine (Tyr; Y). The mechanism of phosphorylation revolves around the side chains of these amino acids. Serine, Threonine and Tyrosine have an -OH group that attacks the terminal phosphate group on ATP, thus transferring a phosphate group to the amino acid side chain. Although this reaction is unidirectional (due to the vast quantity energy released from the conversion of ATP to ADP), phosphorylation of proteins is reversible. Kinases and Phosphatases mediate the reverse reaction via the phosphorylation and dephosphorylation of substrates, respectively. Kinases mediate phosphorylation at Serine, threonine and tyrosine side chains, and phosphatases reverse protein phosphorylation by hydrolyzing the phosphate group.
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