Synthesis and enzymatic evaluation of ketose phosphonates: the interplay between mutarotation, monofluorination and acidity

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DOIResolve DOI: http://doi.org/10.1039/c2sc01077a
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TypeArticle
Journal titleChemical Science
ISSN2041-6520
2041-6539
Volume3
Issue6
Pages18661878
AbstractKetose-phosphonates may adopt open chain, or α- or β-furanosyl, or α- or β-pyranosyl configurational isomers in aqueous solution. An HPLC and NMR analysis of a series of ketose-phosphonates with a thymidylyltransferase (dTDP-glucose pyrophosphorylase) implied a rapid dynamic equilibrium between the pyranosyl forms of gluco-ketose phosphonate leading to efficient production of unique sugar nucleotide analogues. The preparation of diastereomerically pure gluco-configured monofluoromethylenephosphonates enabled the determination of the thymidylyltransferase preference for CHF stereochemistry. The effects of acidity upon thymidylyltransferase substrate specificity were determined using a series of monofluoro- and difluoro- ketose-phosphonates. WaterLOGSY NMR spectroscopy demonstrated a switching of the ordered Bi-Bi mechanism with ketose-phosphonate substrates. Ketose-phosphonates are presented as a unique class of sugar 1-phosphate analogues with potential applications as glycosyltransferase probes.
Publication date
LanguageEnglish
AffiliationNRC Institute for Marine Biosciences; National Research Council Canada
Peer reviewedYes
NPARC number21268964
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Record identifiera5eed3d8-3eef-4700-8252-af257917ae3b
Record created2013-11-28
Record modified2016-05-09
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