Uridine diphosphate(UDP) sugars are essential precursors forglycosylationreactions in all forms of life. Reactions that transfer the carbohydrate from theUDPdonor are catalyzed byglycosyltransferases(Gtfs). Whil
These studies have repeatedly identified the overexpression of uridine diphosphate (UDP)-glycosyltransferases (UGTs) in IR populations across Africa including: An. coluzzii in Nigeria, Niger, Chad, and Burkina Faso18,19; An. gambiae in Burkina Faso20; An. arabiensis in Tanzania (UGT308D1)21; ...
members of this superfamily exhibit structural similarities. Allglycosyltransferaseshave a bidomain structure where the N-terminal domain binds the acceptor (aglycone) substrate and the C-terminal domain binds the donor (nucleotide diphosphate-hexose) substrate. Each domain contains aRossmann foldmotif comp...
expedient access to theΨβ-C-glycoside core structure represents the principal challenge. Methylation at N1 and conversion into the 5′-triphosphates proceed by transformations well implemented for process scale use15,16,17,18,19. Since the first chemical synthesis ...
protein engineeringNatural products have garnered significant attention due to their exceptional industrial and medicinal value. Glycosylation, a crucial structural modification in these products, is typically mediated by uridine diphosphate-dependent glycosyltransferases (UGTs). These enzymes not only enhance ...
ATP-binding cassette (ABC) transporters actively transport various substances across membranes, while uridine diphosphate (UDP) glycosyltransferases (UGTs) are proteins that catalyse the chemical modification of various organic compounds. Both of these protein superfamilies have been associated with conferring...
Uridine diphosphate-dependent glycosyltransferases (UGTs) modify these compounds by covalently adding one or multiple sugar molecules. This glycosylation process converts volatile, unstable, and hydrophobic aroma compounds into hydrophilic, stable, and slow-releasing reservoirs of fruit flavor. The diversity ...
Matyas GR, Morré DJ (1983) Coupling of uridine-5′-diphosphate (UDP) formation and nicotinamide adenine dinucleotide (NAD + ) reduction for cytochemical localization of glycosyltransferases. J Histochem Cytochem 31:1175–1182Matyas, GR, Morré, DJ (1983) Coupling of uridine-5′-diphosphate (UDP...
UDP-glycosyltransferases are known to catalyze the covalently link ofglycosylgroups including UDP-glucuronic acid, UDP-glucose, UDP-galactose, UDP-xylose. UDP-glucuronosyltransferases are a class of UDP-glycosyltransferases utilizing UDP-glucuronic acid as the sugar donor to formglucuronides[...
1. Uridine-diphosphate-N-acetylglucosamine (UDP-GlcNAc) is the sugar nucleotide donor for the synthesis of O-GlcNAc modified proteins, by O-GlcNAc transferase (OGT). OGT has a high affinity for UDP-GlcNAc, which provides it with a competitive advantage over nucleotide transporters in the...