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Chemical Compound Review

CHEBI:29269     trihydroxy-selanylidene- phosphorane

Synonyms: HMDB03840, AC1L1APH, AR-1L0897, AC1Q22ZZ, [P(OH)3Se], ...
 
 
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Disease relevance of trihydroxy-selanylidene-phosphorane

  • In Escherichia coli and Salmonella typhimurium it has been shown that selenophosphate serves as the selenium donor for the conversion of seryl-tRNA to selenocysteyl-tRNA and for the synthesis of 2-selenouridine, a modified nucleoside present in tRNAs [1].
  • A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium [2].
  • Our previous demonstration that a Se(0)-generating system consisting of l-selenocysteine and the Azotobacter vinelandii NifS protein can replace selenide for selenophosphate biosynthesis in vitro suggested a mechanism whereby cells can overcome selenide toxicity [3].
 

High impact information on trihydroxy-selanylidene-phosphorane

 

Chemical compound and disease context of trihydroxy-selanylidene-phosphorane

 

Biological context of trihydroxy-selanylidene-phosphorane

 

Anatomical context of trihydroxy-selanylidene-phosphorane

 

Gene context of trihydroxy-selanylidene-phosphorane

 

Analytical, diagnostic and therapeutic context of trihydroxy-selanylidene-phosphorane

  • This compound, tentatively identified as a selenophosphate [Veres, Z., Tsai, L., Scholz, T. D., Politino, M., Balaban, R. S., & Stadtman, T. C. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2975-2979], is indistinguishable from chemically prepared monoselenophosphate by 31P NMR spectroscopy and ion pairing HPLC [18].

References

  1. Selenophosphate synthetase: detection in extracts of rat tissues by immunoblot assay and partial purification of the enzyme from the archaean Methanococcus vannielii. Kim, I.Y., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. A purified selenophosphate-dependent enzyme from Salmonella typhimurium catalyzes the replacement of sulfur in 2-thiouridine residues in tRNAs with selenium. Veres, Z., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  3. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. Lacourciere, G.M., Mihara, H., Kurihara, T., Esaki, N., Stadtman, T.C. J. Biol. Chem. (2000) [Pubmed]
  4. Selenocysteine. Stadtman, T.C. Annu. Rev. Biochem. (1996) [Pubmed]
  5. Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins. Lacourciere, G.M., Levine, R.L., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  6. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system. Ogasawara, Y., Lacourciere, G., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  7. Synthesis and characterization of selenotrisulfide-derivatives of lipoic acid and lipoamide. Self, W.T., Tsai, L., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  8. Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide. Kim, I.Y., Veres, Z., Stadtman, T.C. J. Biol. Chem. (1992) [Pubmed]
  9. Functional expression in Escherichia coli of the Haemophilus influenzae gene coding for selenocysteine-containing selenophosphate synthetase. Wilting, R., Vamvakidou, K., Böck, A. Arch. Microbiol. (1998) [Pubmed]
  10. Emerging awareness of the critical roles of S-phosphocysteine and selenophosphate in biological systems. Stadtman, T.C. Biofactors (1994) [Pubmed]
  11. Selenoprotein synthesis in archaea. Rother, M., Resch, A., Wilting, R., Böck, A. Biofactors (2001) [Pubmed]
  12. Interleukin-1-induced nuclear factor kappa B activation is inhibited by overexpression of phospholipid hydroperoxide glutathione peroxidase in a human endothelial cell line. Brigelius-Flohé, R., Friedrichs, B., Maurer, S., Schultz, M., Streicher, R. Biochem. J. (1997) [Pubmed]
  13. Structural and functional investigation of a putative archaeal selenocysteine synthase. Kaiser, J.T., Gromadski, K., Rother, M., Engelhardt, H., Rodnina, M.V., Wahl, M.C. Biochemistry (2005) [Pubmed]
  14. A DNA replication-related element downstream from the initiation site of Drosophila selenophosphate synthetase 2 gene is essential for its transcription. Jin, J.S., Baek, S., Lee, H., Oh, M.Y., Koo, Y.E., Shim, M.S., Kwon, S.Y., Jeon, I., Park, S.Y., Baek, K., Yoo, M.A., Hatfield, D.L., Lee, B.J. Nucleic Acids Res. (2004) [Pubmed]
  15. Effects of monovalent cations and divalent metal ions on Escherichia coli selenophosphate synthetase. Kim, I.Y., Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  16. The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphate. Lacourciere, G.M., Stadtman, T.C. J. Biol. Chem. (1998) [Pubmed]
  17. Selenophosphate as a substrate for mammalian selenocysteine synthase, its stability and toxicity. Mizutani, T., Kanaya, K., Tanabe, K. Biofactors (1999) [Pubmed]
  18. Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX. Glass, R.S., Singh, W.P., Jung, W., Veres, Z., Scholz, T.D., Stadtman, T.C. Biochemistry (1993) [Pubmed]
 
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