147072-52-4Relevant articles and documents
Synthesis of Cell-Permeable N-Acetylhexosamine 1-Phosphates
Capota, Emanuela,Kakde, Badrinath N.,Kohler, Jennifer J.,Tambar, Uttam K.
, p. 18257 - 18264 (2021/10/25)
We recently reported the incorporation of diazirine photo-cross-linkers onto the O-GlcNAc posttranslational modification in mammalian cells, enabling the identification of binding partners of O-GlcNAcylated proteins. Unfortunately, the syntheses of the diazirine-functionalized substrates have exhibited inconsistent yields. We report a robust and stereoselective synthesis of cell-permeable GlcNAc-1-phosphate esters based on the use of commercially available bis(diisopropylamino)chlorophosphine. We demonstrate this approach for two diazirine-containing GlcNAc analogues, and we report the cellular incorporation of these compounds into glycoconjugates to support photo-cross-linking applications.
A very simple synthesis of GlcNAc-α-pyrophosphoryl-decanol: A substrate for the assay of a bacterial galactosyltransferase
Brockhausen, Inka,Larsson, E. Andreas,Hindsgaul, Ole
, p. 804 - 807 (2008/09/18)
Lipid-linked sugar pyrophosphates, such as GlcNAc-pyrophosphoryl undecaprenol, are important intermediates in the biosynthesis of cell-surface bacterial polysaccharides. It was recently demonstrated that much simpler lipids could substitute for undecaprenol while retaining biological activity, thus making efficient synthetic access to this class of compounds highly desirable. In order to facilitate the synthesis of pure substrates for bacterial glycosyltransferases, we have developed a simple 'two-pot' synthesis which we demonstrate here for GlcNAc-α-pyrophosphoryl-decanol (4). GlcNAc pyrophosphate, produced by mild periodate oxidation/β-elimination of commercial UDP-GlcNAc, is alkylated using 1-iododecane to yield the target compound 4 in 39% yield. Compound 4 is shown to be an efficient acceptor for a bacterial galactosyltransferase.
Identification of a UDP-Gal: GlcNAc-R galactosyltransferase activity in Escherichia coli VW187
Montoya-Peleaz, Pedro J.,Riley, John G.,Szarek, Walter A.,Valvano, Miguel A.,Schutzbach, John S.,Brockhausen, Inka
, p. 1205 - 1211 (2007/10/03)
A novel acceptor substrate for galactosyltransferase was synthesized containing GlcNAcα-pyrophosphate, covalently bound to a hydrophobic phenoxyundecyl moiety (GlcNAc α-O-PO3-PO3-(CH 2)11-O-Phenyl). The new subs
