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Phosphoserine


Phosphoserine (abbreviated as SEP or J) is an ester of serine and phosphoric acid. Phosphoserine is a component of many proteins as the result of posttranslational modifications. The phosphorylation of the alcohol functional group in serine to produce phosphoserine is catalyzed by various types of kinases. Through the use of technologies that utilize an expanded genetic code, phosphoserine can also be incorporated into proteins during translation.

It is a normal metabolite found in human biofluids.

Phosphoserine has three potential coordination sites (carboxyl, amine and phosphate group) Determination of the mode of coordination between phosphorylated ligands and metal ions occurring in an organism is a first step to explain the function of the phosphoserine in bioinorganic processes.

References

References

  1. (2006-03-11). "Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks". Cell.
  2. Krebs, Edwin G.. (1985-10-01). "The phosphorylation of proteins: a major mechanism for biological regulation". Biochemical Society Transactions.
  3. (2002-12-06). "The Protein Kinase Complement of the Human Genome". Science.
  4. (2011-08-26). "Expanding the Genetic Code of Escherichia coli with Phosphoserine". Science.
  5. (2015-01-01). "Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog". Nature Chemical Biology.
  6. (2015-09-09). "Robust production of recombinant phosphoproteins using cell-free protein synthesis". Nature Communications.
  7. (1993). "Analysis of free and bound O-phosphoamino acids in urine by gas chromatography with flame photometric detection". Biomedical Chromatography.
  8. (2009-03-10). "Coordination mode in the binary systems of copper(II)/O-phospho-L-serine". Journal of Coordination Chemistry.
  9. Jastrzab, Renata. (2009-05-01). "Phosphoserine and specific types of its coordination in copper(II) and adenosine nucleotides systems – Potentiometric and spectroscopic studies". Journal of Inorganic Biochemistry.
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