Enzymatic approach to unnatural glycosides with diverse aglycon scaffolds using glycosyltransferase VinC.
Glycosyltransferase VinC was explored for a construction of glycoside libraries using dTDP-vicenisamine and structurally unrelated unnatural aglycons, and new unnatural vicenisaminides were successfully constructed. Structural elements of aglycon recognition by VinC were proposed by modeling studies and were confirmed by the success of transglycosylation upon a designed aglycon.
Minami
Atsushi
A
Department of Chemistry and Department of Chemistry and Materials Science, Tokyo Institute of Technology, 2-12-1, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
Uchida
Rei
R
Eguchi
Tadashi
T
Kakinuma
Katsumi
K
D006027:Glycosides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D016695:Glycosyltransferases / Q000737:chemistry* / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D013329:Structure-Activity Relationship
D006027:Glycosides; D016695:Glycosyltransferases