Journal article
Monoselenophosphate: Synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX
Biochemistry (Easton), Vol.32(47), pp.12555-12559
11/01/1993
DOI: 10.1021/bi00210a001
PMID: 8251472
Abstract
A labile, selenium donor compound required for synthesis of selenium-dependent enzymes and seleno-tRNAs is formed from ATP and selenide by the SELD enzyme. 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. Furthermore, addition of chemically prepared monoselenophosphate caused a dose-dependent decrease in the amount of 75Se incorporated into tRNAs from 75SePX generated in situ by SELD enzyme. A procedure is described for the chemical synthesis of monoselenophosphate in which the readily prepared (MeO)3PSe is converted in quantitative yield to (TMSO)3PSe followed by complete cleavage of the latter to monoselenophosphate in oxygen-free aqueous buffer. The chemical properties of chemically synthesized monoselenophosphate are described.
Details
- Title: Subtitle
- Monoselenophosphate: Synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX
- Creators
- Richard S GlassWaheguru P SinghWoncheol JungZsuzsa VeresThomas D ScholzThressa Stadtman
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.32(47), pp.12555-12559
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi00210a001
- PMID
- 8251472
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 11/01/1993
- Academic Unit
- Cardiology; Stead Family Department of Pediatrics; Fraternal Order of Eagles Diabetes Research Center; Child and Community Health
- Record Identifier
- 9984093311802771
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