Phosphorylation

Serine in an amino acid chain, before and after phosphorylation.

In biochemistry, phosphorylation is described as the "transfer of a phosphate group" from a donor to an acceptor.[1] A common phosphorylating agent (phosphate donor) is ATP and a common family of acceptor are alcohol (chemistry)s:

[Adenosyl−O−PO2−O−PO2−O−PO3]4− + ROH → Adenosyl−O−PO2−O−PO3H]2− + [RO−P−O3]2−

This equation can be written in several ways that are nearly equivalent that describe the behaviors of various protonated states of ATP, ADP, and the phosphorylated product. As is clear from the equation, a phosphate group per se is not transferred, but a phosphoryl group (PO3-). Phosphoryl is an electrophile.[2] This process and its inverse, dephosphorylation, are common in biology.[3] Protein phosphorylation often activates (or deactivates) many enzymes.[4][5]

  1. ^ "phosphorylation". IUPAC Gold Book.
  2. ^ Adams, Joseph A. (2001). "Kinetic and Catalytic Mechanisms of Protein Kinases". Chemical Reviews. 101 (8): 2271–2290. doi:10.1021/cr000230w. PMID 11749373.
  3. ^ Chen J, He X, Jakovlić I (November 2022). "Positive selection-driven fixation of a hominin-specific amino acid mutation related to dephosphorylation in IRF9". BMC Ecology and Evolution. 22 (1): 132. doi:10.1186/s12862-022-02088-5. PMC 9650800. PMID 36357830. S2CID 253448972. Text was copied from this source, which is available under a Creative Commons Attribution 4.0 International License.
  4. ^ Oliveira AP, Sauer U (March 2012). "The importance of post-translational modifications in regulating Saccharomyces cerevisiae metabolism". FEMS Yeast Research. 12 (2): 104–117. doi:10.1111/j.1567-1364.2011.00765.x. PMID 22128902.
  5. ^ Tripodi F, Nicastro R, Reghellin V, Coccetti P (April 2015). "Post-translational modifications on yeast carbon metabolism: Regulatory mechanisms beyond transcriptional control". Biochimica et Biophysica Acta (BBA) - General Subjects. 1850 (4): 620–627. doi:10.1016/j.bbagen.2014.12.010. hdl:10281/138736. PMID 25512067.

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