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Phosphoserine information


l-Phosphoserine
Skeletal formula
Ball-and-stick model
Names
IUPAC name
(S)-2-Amino-3-(phosphonooxy)propionic acid
Identifiers
CAS Number
  • 407-41-0 checkY
3D model (JSmol)
  • Interactive image
ChEBI
  • CHEBI:15811 checkY
ChEMBL
  • ChEMBL284377 checkY
ChemSpider
  • 62074 checkY
DrugBank
  • DB04522 checkY
ECHA InfoCard 100.006.352 Edit this at Wikidata
EC Number
  • 206-986-0
IUPHAR/BPS
  • 1411
KEGG
  • C01005
MeSH Phosphoserine
PubChem CID
  • 106
UNII
  • VI4F0K069V checkY
CompTox Dashboard (EPA)
  • DTXSID1046348 Edit this at Wikidata
InChI
  • InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 checkY
    Key: BZQFBWGGLXLEPQ-REOHCLBHSA-N checkY
  • InChI=1/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1
SMILES
  • O=P(O)(O)OC[C@@H](C(=O)O)N
Properties
Chemical formula
C3H8NO6P
Molar mass 185.073 g/mol
Melting point 228 °C (442 °F; 501 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

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.[1] The phosphorylation of the alcohol functional group in serine to produce phosphoserine is catalyzed by various types of kinases.[2][3] Through the use of technologies that utilize an expanded genetic code, phosphoserine can also be incorporated into proteins during translation.[4][5][6]

It is a normal metabolite found in human biofluids.[7]

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.[8][9]

  1. ^ Olsen, Jesper V.; Blagoev, Blagoy; Gnad, Florian; Macek, Boris; Kumar, Chanchal; Mortensen, Peter; Mann, Matthias (2006-03-11). "Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  2. ^ Krebs, Edwin G. (1985-10-01). "The phosphorylation of proteins: a major mechanism for biological regulation". Biochemical Society Transactions. 13 (5): 813–820. doi:10.1042/bst0130813. PMID 2998902.
  3. ^ Manning, G.; Whyte, D. B.; Martinez, R.; Hunter, T.; Sudarsanam, S. (2002-12-06). "The Protein Kinase Complement of the Human Genome". Science. 298 (5600): 1912–1934. Bibcode:2002Sci...298.1912M. doi:10.1126/science.1075762. PMID 12471243. S2CID 26554314.
  4. ^ Park, Hee-Sung; Hohn, Michael J.; Umehara, Takuya; Guo, Li-Tao; Osborne, Edith M.; Benner, Jack; Noren, Christopher J.; Rinehart, Jesse; Söll, Dieter (2011-08-26). "Expanding the Genetic Code of Escherichia coli with Phosphoserine". Science. 333 (6046): 1151–1154. Bibcode:2011Sci...333.1151P. doi:10.1126/science.1207203. PMC 5547737. PMID 21868676.
  5. ^ Rogerson, Daniel T; Sachdeva, Amit; Wang, Kaihang; Haq, Tamanna; Kazlauskaite, Agne; Hancock, Susan M; Huguenin-Dezot, Nicolas; Muqit, Miratul M K; Fry, Andrew M (2015-01-01). "Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog". Nature Chemical Biology. 11 (7): 496–503. doi:10.1038/nchembio.1823. PMC 4830402. PMID 26030730.
  6. ^ Oza, Javin P.; Aerni, Hans R.; Pirman, Natasha L.; Barber, Karl W.; ter Haar, Charlotte M.; Rogulina, Svetlana; Amrofell, Matthew B.; Isaacs, Farren J.; Rinehart, Jesse (2015-09-09). "Robust production of recombinant phosphoproteins using cell-free protein synthesis". Nature Communications. 6: 8168. Bibcode:2015NatCo...6.8168O. doi:10.1038/ncomms9168. PMC 4566161. PMID 26350765.
  7. ^ Kataoka, H; Nakai, K; Katagiri, Y; Makita, M (1993). "Analysis of free and bound O-phosphoamino acids in urine by gas chromatography with flame photometric detection". Biomedical Chromatography. 7 (4): 184–8. doi:10.1002/bmc.1130070403. PMID 7693088.
  8. ^ Jastrzab, Renata; Lomozik, Lechoslaw (2009-03-10). "Coordination mode in the binary systems of copper(II)/O-phospho-L-serine". Journal of Coordination Chemistry. 62 (5): 710–720. doi:10.1080/00958970802317855. S2CID 95207026.
  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. 103 (5): 766–773. doi:10.1016/j.jinorgbio.2009.01.012. PMID 19230980.

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Phosphoserine

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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...

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Serine

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ketone by phosphoserine transaminase (EC 2.6.1.52) yields 3-phosphoserine (O-phosphoserine) which is hydrolyzed to serine by phosphoserine phosphatase...

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Glycosylation

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such as ceramide. Phosphoglycans linked through the phosphate of a phosphoserine. C-linked glycans, a rare form of glycosylation where a sugar is added...

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Phosphoserine phosphatase

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The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction O-phospho-L(or D)-serine + H2O ⇌ {\displaystyle \rightleftharpoons } L(or D)-serine...

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Phosphoserine transaminase

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Phosphoserine transaminase (EC 2.6.1.52, PSAT, phosphoserine aminotransferase, 3-phosphoserine aminotransferase, hydroxypyruvic phosphate-glutamic transaminase...

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Phospholipid

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(ammonium salt) Phosphatidylglycerol DLPS-NA 1,2-Dilauroyl-sn-glycero-3-phosphoserine (sodium salt) Phosphatidylserine DMPA-NA 80724-3 1...

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Biosynthesis

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the enzyme phosphoserine aminotransferase, which transfers an amino group from glutamate onto 3-phosphonooxypyruvate to yield L-phosphoserine. The final...

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Phosphoprotein

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been proposed as biomarkers for breast cancer. Protein phosphorylation Phosphoserine Keyword - Phosphoprotein Phosphoproteins in extracellular vesicles as...

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PSPH

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Phosphoserine phosphatase is an enzyme that in humans is encoded by the PSPH gene. The protein encoded by this gene belongs to a subfamily of the phosphotransferases...

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Methionine

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CysM in E. coli), but in Aeropyrum pernix and some other archaea O-phosphoserine is used. CysK and CysM are homologues, but belong to the PLP fold type...

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PSAT1

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Phosphoserine aminotransferase (PSA) also known as phosphohydroxythreonine aminotransferase (PSAT) is an enzyme that in humans is encoded by the PSAT1...

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Protein phosphatase

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Phosphotyrosine Serine-/threonine-specific phosphatases PP2C (PPP2CA) Phosphoserine/-threonine Dual specificity phosphatases VHR, DUSP1–DUSP28...

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Glycoprotein

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hydroxyproline. In P-glycosylation, sugars are attached to phosphorus on a phosphoserine. In C-glycosylation, sugars are attached directly to carbon, such as...

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Tyrosine

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reliable protein-protein interactions—by means of phosphotyrosine, phosphoserine and phosphothreonine. Binding sites for a signalling phosphoprotein...

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Protein metabolism

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3-phosphohydroxypyruvate (3-phosphoglycerate dehydrogenase) → 3-phosphoserine (aminotransferase) → Serine (phosphoserine phosphatase) Threonine§ CH3-CH(OH)- Aspartate →...

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Fluoride

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et al. (2002). "Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states". J...

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Selenocysteine

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AM, Whitman WB, Söll D (December 2006). "RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea". Proceedings of the...

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KIAA0232

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KIAA0232 is a nuclear phosphoserine protein which in humans is encoded by the KIAA0232 gene. KIAA0232 is located at 4p16.1 neighboring TBC1 domain family...

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International Working Group on Neurotransmitter Related Disorders

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dihydrofolate reductase, 3-phosphoglycerate dehydrogenase, 3-phosphoserine phosphatase, phosphoserine aminotransferase, the glycine cleavage system (the deficiency...

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Chromosome 7

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subunit p20 PPP1R17: protein phosphatase 1 regulatory subunit 17 PSPH: phosphoserine phosphatase PURB: purine-rich element binding protein B PVRIG: encoding...

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PIN1

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Lu PJ, Zhou XZ, Shen M, Lu KP (Feb 1999). "Function of WW domains as phosphoserine- or phosphothreonine-binding modules". Science. 283 (5406): 1325–8....

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