Editing Phosphorylation (section)

{{Short description|Chemical process of introducing a phosphate}}
[[File:Phosporylation of a serine residue, before and after shot.png|thumb|[[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.<ref name="ana&physio">{{cite web |title=phosphorylation|url=https://goldbook.iupac.org/terms/view/PT06790|website=IUPAC Gold Book}}</ref>  A common phosphorylating agent (phosphate donor) is [[Adenosine triphosphate|ATP]] and a common family of acceptor are [[Alcohol (Chemistry)|alcohol]]s:
:{{chem2|[Adenosyl\sO\sPO2\sO\sPO2\sO\sPO3](4-)  +  ROH  ->  Adenosyl\sO\sPO2\sO\sPO3H](2-)  +  [RO\sP\sO3](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 (PO<sub>3</sub><sup>-</sup>).  '''Phosphoryl''' is an [[electrophile]].<ref name=Ahn>{{cite journal |doi=10.1021/cr000230w |title=Kinetic and Catalytic Mechanisms of Protein Kinases |date=2001 |last1=Adams |first1=Joseph A. |journal=Chemical Reviews |volume=101 |issue=8 |pages=2271–2290 |pmid=11749373 }}</ref>
This process and its inverse, [[dephosphorylation]], are common in [[biology]].<ref name="Chen-2022">{{cite journal |vauthors=Chen J, He X, Jakovlić I |date=November 2022 |title=Positive selection-driven fixation of a hominin-specific amino acid mutation related to dephosphorylation in IRF9 |journal=BMC Ecology and Evolution |volume=22 |issue=1 |pages=132 |doi=10.1186/s12862-022-02088-5 |pmid=36357830 |pmc=9650800 |s2cid=253448972 |doi-access=free }} [[File:CC-BY_icon.svg|50x50px]]  Text was copied from this source, which is available under a [[creativecommons:by/4.0/|Creative Commons Attribution 4.0 International License]].</ref> [[Protein phosphorylation]] often activates (or deactivates) many [[enzyme]]s.<ref>{{cite journal | vauthors = Oliveira AP, Sauer U | title = The importance of post-translational modifications in regulating Saccharomyces cerevisiae metabolism | journal = FEMS Yeast Research | volume = 12 | issue = 2 | pages = 104–117 | date = March 2012 | pmid = 22128902 | doi = 10.1111/j.1567-1364.2011.00765.x | doi-access = free }}</ref><ref>{{cite journal | vauthors = Tripodi F, Nicastro R, Reghellin V, Coccetti P | title = Post-translational modifications on yeast carbon metabolism: Regulatory mechanisms beyond transcriptional control | journal = Biochimica et Biophysica Acta (BBA) - General Subjects | volume = 1850 | issue = 4 | pages = 620–627 | date = April 2015 | pmid = 25512067 | doi = 10.1016/j.bbagen.2014.12.010 | hdl = 10281/138736 | hdl-access = free }}</ref>