Glycosides articles from across Nature Portfolio

Uridine diphosphate-dependent glycosyltransferases (UGTs) play a vital role in the biocatalytic glycosylation of phenolic compounds, however, UGT-catalyzed transformations remain not well-characterized. Here, the authors investigate new members of UGT72 and UGT84 families, revealing their specific reactivity and regio-selectivity on selected polyphenolic substrates.

The Suzuki-Miyaura cross-coupling of glycal boronates stands out for its reliability, wide availability, and non-toxic nature, but the stability of glycal donor has hindered progress in this field. Herein, the authors report palladium-catalyzed glycal-based Suzuki-Miyaura reaction using stable glycal boronates, overcoming the stability issue.

Mucins are glycosylated proteins with important biological functions such as protection. Although glycopeptidases can cleave them, dedicated hydrolytic enzymes specific for mucins were unknown. Now microbial mucinases are discovered that specifically recognize mucin O-glycan clusters and employ two glutamic acid residues for catalytic cleavage.

Biological degradation of glycosides involves, alongside hydrolysis, β-elimination for glycosidic bond cleavage. Here, the authors report an O-glycoside β-eliminase from Agrobacterium tumefaciens that converts the C3-oxidized O-β-d-glucoside of phloretin into the aglycone and the 2-hydroxy-3-keto-d-glycal elimination product, and suggest convergent evolution of β-eliminase active sites for the cleavage of natural product 3-keto-O-glycosides.

Pseudouridine (Ψ), the C-nucleoside isomer of uridine, and its 1-N-methyl derivative, are incorporated in mRNA vaccines and essential for their efficiency, but difficult to synthetically access. Here, the authors report on selective and atom-economic 1N-5C rearrangement of β-d-ribosyl on uracil to obtain Ψ from unprotected U in quantitative yield

Gut microbes have enzymes that break down the heavily glycosylated mucin protein of host animals, but known enzymes recognize only one glycan chain. Now, bioinformatic exploration has uncovered a family of mucinases that targets dense sugar residues.

The biological functions of glycan motifs such as the Lewis blood antigens are often defined by their precise multivalent presentation on complex glycoconjugates, making synthesis particularly challenging. Access to a number of positionally defined Lewis motifs on natural polysaccharide scaffolds has now been achieved using bacterial glycosyltransferases.