Synthesis of C-glycosyl phosphonate derivatives of 4-amino-4-deoxy-α-ʟ-arabinose

• Lukáš Kerner and
• Paul Kosma

Beilstein J. Org. Chem. 2020, 16, 9–14, doi:10.3762/bjoc.16.2

• have frequently been exploited as potential inhibitors for glycosyl transferases since the carbon–phosphorus bond is not hydrolyzed in the active site of glycosyl transferases [10][11][12][13]. Herein, we report on the synthesis of α-anomeric C-arabinosyl methylphosphonate ester derivatives as model

Synthetic and semi-synthetic approaches to unprotected N-glycan oxazolines

• Antony J. Fairbanks

Beilstein J. Org. Chem. 2018, 14, 416–429, doi:10.3762/bjoc.14.30

• use of the ENGase Endo A, and separated by careful chromatography on a carbon-Celite® column. Although Wang and co-workers did not at that time report the conversion of these glycans into the corresponding oxazolines, the basic Man5GlcNAc structure has since been extended using a sequence of glycosyl

• transferases (namely a β(1–2)-GlcNAc transferase, a β(1–4)-galactosyltransferase, and an α(2–6)-sialyltransferase), and the corresponding hybrid N-glycan oxazoline used as a substrate for ENGases [110]. Conclusion N-Glycan oxazolines have found widespread use as activated donor substrates for ENGase enzymes, a

Strategies toward protecting group-free glycosylation through selective activation of the anomeric center

• A. Michael Downey and
• Michal Hocek

Beilstein J. Org. Chem. 2017, 13, 1239–1279, doi:10.3762/bjoc.13.123

• and its increasing popularity, we briefly highlight the power of this reagent not only in the capacity of glycosylation as an anomeric activator, but also as a phosphate activator to form diphosphates. We selected one example of their work because it also showcases the use of glycosyl transferases in

Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience

• Serge Pérez and
• Daniele de Sanctis

Beilstein J. Org. Chem. 2017, 13, 1145–1167, doi:10.3762/bjoc.13.114

• of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures

• hydrolases; glycosyl transferases; kinetic crystallography; lectins; polysaccharides; powder diffraction; small-angle X-ray scattering; starch; synchrotron radiation; transporters; X-ray crystallography; Introduction Over the last decade, glycoscience has greatly benefited from the development of structural

• have been solved over the last 25 years, with a particular emphasis on the number of structures determined at high resolution. Glycosyl transferases: The biosynthesis of oligosaccharides is performed by a ubiquitous class of enzymes: the glycosyl transferases (GTs). The catalytic mechanism underlying

Polyketide stereocontrol: a study in chemical biology

• Kira J. Weissman

Beilstein J. Org. Chem. 2017, 13, 348–371, doi:10.3762/bjoc.13.39

• intermediate (6-deoxyerythronolide B in the case of erythromycin biosynthesis, Figure 3) is then frequently modified by a series of so-called ‘post-PKS enzymes’ (e.g., methyl transferases, hydroxylases, and glycosyl transferases), to achieve its final bioactive form [10]. Nature has, in fact, evolved two