Novel aspects of interaction between UDP-gal and GlcNAc beta-1,4-galactosyltransferase: transferability and remarkable inhibitory activity of UDP-(mono-O-methylated gal), UDP-Fuc and UDP-man.
Four mono-O-methylated and one mono-O-acetylated UDP-D-Gal analogues and UDP-L-Fuc were synthesized. 2-O-Methyl-D-galactose residue was enzymatically transferred to give 2'-O-methyllactosaminide in high yield. UDP-Fuc and UDP-Man showed potent inhibitory activities against beta-1,4-galactosyltransferase. Structural requirement and steric allowance for the ground and transition states of the enzyme reaction were discussed.
Endo
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Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Kajihara
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Y
Kodama
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Hashimoto
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D005643:Fucose / Q000494:pharmacology*; D005700:Galactosyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D014531:Uridine Diphosphate Galactose / Q000378:metabolism* / Q000494:pharmacology; D014539:Uridine Diphosphate Sugars / Q000494:pharmacology*
D014539:Uridine Diphosphate Sugars; C042056:uridine diphosphate mannose; D005643:Fucose; D014531:Uridine Diphosphate Galactose; D005700:Galactosyltransferases; C067546:N-acetylglucosamine 4-beta-galactosyltransferase