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In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. [1] This process and its inverse, dephosphorylation , are common in biology . [ 2 ] Protein phosphorylation often activates (or deactivates) many enzymes .
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its ...
The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. In the case of glucose, the product of this phosphorylation is glucose-6-phosphate (Glc-6P). Due to the negative charge of the phosphate, this Glc-6P can no longer freely leave the cell.
The structures of some autophosphorylation complexes are known from crystals of protein kinases in which the phosphorylation site (Ser, Thr, or Tyr) of one monomer in the crystal is sitting in the active site of another monomer of the crystal in a manner similar to known peptide-substrate/kinase structures. [6]
Cks1-dependent multi-phosphorylation occurs in a processive or semi-processive manner, evidenced by the lack of intermediate Sic1 phosphorylation states in normal cells. This processivity is also dependent on the presence of the cyclin docking site since increasing the numbers of mutations in this site decreases the net phosphorylation rate.
Phosphorylation is a key reversible modification that regulates protein function, subcellular localization, complex formation, degradation of proteins and therefore cell signaling networks. With all of these modification results, it is estimated that between 30–65% of all proteins may be phosphorylated, some multiple times.
Protein phosphorylation is a very important and frequent post-translational modification that can impact a protein's localization, stability, and whether or not it can dimerize or form stable bonds with other substances. It is vital to pinpoint which amino acid in the protein’s primary structure is being phosphorylated in order to understand ...
The "phosphoryl" group plays a central role in phosphorylation. In biochemical reactions involving phosphate groups (e.g. adenosine triphosphate), a "phosphoryl" group is usually transferred between the substrates by the "phosphoryl transfer reactions" (see phosphorylation).