Glycoside phosphorylases (EC 2.4.xx) carry out the reversible phosphorolysis of glucan
polymers, producing the corresponding sugar 1-phosphate and a shortened glycan chain. β-1,3-…

Glycoside phosphorylases catalyse the reversible synthesis of glycosidic bonds by
glycosylation with concomitant release of inorganic phosphate. The equilibrium position of such …

Chronic infections with Pseudomonas aeruginosa are associated with the formation of
bacterial biofilms. The tetrameric P. aeruginosa lectin LecA is a virulence factor and an anti-…

Next-generation COVID-19 vaccines are critical due to the ongoing evolution of SARS-CoV-2
virus and rapid waning duration of the neutralizing antibody response against current …

Bacterial adhesion, biofilm formation and host cell invasion of the ESKAPE pathogen
Pseudomonas aeruginosa require the tetravalent lectins LecA and LecB, which are therefore drug …

Glycoside phosphorylases (GPs) catalyze the phosphorolysis of glycans into the corresponding
sugar 1-phosphates and shortened glycan chains. Given the diversity of natural β-(1→3)-…

Glycoside phosphorylases (GPs) carry out a reversible phosphorolysis of carbohydrates into
oligosaccharide acceptors and the corresponding sugar 1‐phosphates. The reversibility of …

Glycoside phosphorylases (GPs) with specificity for β‐(1 → 3)‐gluco‐oligosaccharides are
potential candidate biocatalysts for oligosaccharide synthesis. GPs with this linkage …

Carbohydrate-protein interactions are key for cell-cell and host-pathogen recognition and
thus, emerged as viable therapeutic targets. However, their hydrophilic nature poses major …

Because of the antimicrobial resistance crisis, lectins are considered novel drug targets.
Pseudomonas aeruginosa utilizes LecA and LecB in the infection process. Inhibition of both …