Substrate flexibility of a 2,6-dideoxyglycosyltransferase

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, ena...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2006-01 (35), p.3738-3740
Hauptverfasser: Jakeman, David L, Borissow, Charles N, Graham, Cathy L, Timmons, Shannon C, Reid, Taryn R, Syvitski, Ray T
Format: Artikel
Sprache:eng
Schlagworte:
Glycosyltransferases - chemistry
Hexoses - chemistry
Isoquinolines - chemistry
Magnetic Resonance Spectroscopy - methods
Molecular Conformation
Monosaccharides - chemistry
Sensitivity and Specificity
Stereoisomerism
Substrate Specificity
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Beschreibung
Zusammenfassung: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/b608847c