The following amino acids can be phosphorylated: serine, threonine and tyrosine. The full explanation behind the phosphorylations can be found here: http://www.biochem.umd.edu/biochem/kahn/teach_res/amino_acids/
Another site which provides a graphical summary: http://www.bio.davidson.edu/courses/Molbio/aatable.html
Hope this helps.
2007-01-27 21:26:52
·
answer #1
·
answered by soul83 2
·
1⤊
0⤋
Serine, threonine and tyrosine are the most usual ones.
The products are phosphoesters
Also Histidine and Aspartate are phosphorylared in prokaryotes and some eukaryotes. This type of phosphorylation is the dominant type in prokaryotic two-component signal transduction systems.
Phopho-histidine has a phosphoamide bond and phospho-aspartate a mixed acid anhydride bond (from phosphoric and aspartic acid).
Why? Simply because they are the only amino acids with a functional chemical group that can react with phosphate.
Well glutamate, cysteine, lysine and arginine could also react in theory but I am not aware of any such cases, at least not general enough.
2007-01-28 08:11:17
·
answer #2
·
answered by bellerophon 6
·
2⤊
0⤋
This Site Might Help You.
RE:
What amino acids can be phosphorylated and why?
2015-08-18 09:05:00
·
answer #3
·
answered by Miyoko 1
·
0⤊
0⤋
Serine, Threonine, and Tyrosine = hydroxyl group (-OH) to react with phosphate group
2014-02-21 08:13:24
·
answer #4
·
answered by Anonymous
·
0⤊
0⤋