87906-03-4Relevant academic research and scientific papers
Synthetic potential of fucosyltransferase III for the synthesis of fluorescent-labeled milk oligosaccharides
Rabbani, Said,Compostella, Federica,Franchini, Laura,Wagner, Beatrice,Panza, Luigi,Ernst, Beat
, p. 789 - 807 (2007/10/03)
Various fundamental biologic roles of milk oligosaccharides have been recognized; however, their structure-affinity relationship is still not fully revealed. Herein, we describe the synthesis of the fluorescent-labeled milk oligosaccharides 3-(5-dimethyla
Rational design, synthesis, and characterization of novel inhibitors for human β1,4-galactosyltransferase
Takaya, Kenji,Nagahori, Noriko,Kurogochi, Masaki,Furuike, Tetsuya,Miura, Nobuaki,Monde, Kenji,Lee, Yuan Chuan,Nishimura, Shin-Ichiro
, p. 6054 - 6065 (2007/10/03)
An affinity labeling reagent, uridine 5′-(6-amino-{2-[(7-bromomethyl- 2-naphthyl)methoxycarbonylmethoxy]ethoxy}acetyl-6-deoxy-α-D- galactopyranosyl) diphosphate (1a), was designed on the basis of 3D docking simulation and synthesized to investigate the functional role of Trp310 residue located in the small loop near the active site of human recombinant galactosyltransferase (βGalT-1). Mass spectrometric analysis revealed that the Trp310 residue of βGalT1 can be selectively modified with the naphthylmethyl group of compound 1a at the C-3 position of the indole ring. This result motivated us to synthesize novel uridine-5′-diphosphogalactose (UDP-Gal) analogues as candidates for mechanism-based inhibitors for βGalT-1. We found that uridine 5′-(6-O-[10-(2-naphthyl)-3,6,9- trioxadecanyl]-α-D-galactopyranosyl) diphosphate (2) is the strongest inhibitor (Ki = 1.86 μM) against UDP-Gal (Km, = 4.91 μM) among compounds reported previously. A cold spray ionization time-of-flight mass spectrometry study demonstrated that the complex of this inhibitor and βGalT-1 cannot interact with an acceptor substrate in the presence of Mn2+.
Chemo-enzymatic synthesis of glycopolymers and sequential glycopeptides bearing lactosamine and sialyl Lewisx unit pendant chains
Sallas, Florence,Nishimura, Shin-Ichiro
, p. 2091 - 2103 (2007/10/03)
A variety of glycoconjugates bearing either N-acetyllactosamine or sialyl Lewisx units have been synthesised in a chemo-enzymatic way. This includes the synthesis of glycopolymer copolymerised with acrylamide and whose glucosamine unit was substituted with different kinds of side-chain. Glycopeptides with different spacer-arm glucosamine units have also been prepared and polymerised. The sugar chain was then elongated using glycosyl transferases to afford the novel sequential glycopeptides. In these cases, the polymeric sugar cluster effect led to enzymatic glycosylation with high efficiency. Nevertheless, some differences have been noticed depending on the reaction conditions used for each substrate.
Chemical synthesis of N-acetylglucosamine derivatives and their use as glycosyl acceptors by the Mesorhizobium loti chitin oligosaccharide synthase NodC
Kamst, Eric,Zegelaar-Jaarsveld, Korien,Van Der Marel, Gijs A.,Van Boom, Jacques H.,Lugtenberg, Ben J.J.,Spaink, Herman P.
, p. 176 - 189 (2007/10/03)
Rhizobial bacteria synthesize lipo-chitin oligosaccharide signal molecules (Nod factors) that are essential for the formation of symbiotic organs on the roots of host plants, a process known as nodulation. Biosynthesis of the chitin oligosaccharide moiety
