Substrate flexibility of a 2,6-dideoxyglycosyltransferase.
We report the first 2,6-dideoxysugar-O-glycosyltransferase with substrate flexibility at the 2 position, confirm the function of a putative NDP-hexose 2,3-dehydratase in the jadomycin B biosynthetic gene cluster and deduce the substrate flexibility of downstream enzymes in l-digitoxose assembly, enabling reprogramming of biosynthetic gene clusters to modify sugar substituents.
Jakeman
David L
DL
College of Pharmacy, Dalhousie University, 5968 College St., Halifax, Nova Scotia, Canada. david.jakeman@dal.ca
Borissow
Charles N
CN
Graham
Cathy L
CL
Timmons
Shannon C
SC
Reid
Taryn R
TR
Syvitski
Ray T
RT
D016695:Glycosyltransferases / Q000737:chemistry*; D006601:Hexoses / Q000737:chemistry; D007546:Isoquinolines / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008968:Molecular Conformation; D009005:Monosaccharides / Q000737:chemistry; D012680:Sensitivity and Specificity; D013237:Stereoisomerism; D013379:Substrate Specificity
D006601:Hexoses; C519266:ILEVS1080; D007546:Isoquinolines; D009005:Monosaccharides; C081750:jadomycin B; C020615:digitoxose; D016695:Glycosyltransferases