title: SorF: a glycosyltransferase with promiscuous donor substrate specificity in vitro.
abstract: Glycosylations are well-established steps in numerous biosynthetic pathways, and the attached sugar moieties often influence the specificity or pharmacology of the modified compounds. The sorangicins belong to the polyketide family of natural products, and exhibit antibiotic activity through inhibition of bacterial RNA polymerase. We have identified the sorangicin biosynthetic gene cluster in the producing myxobacterium Sorangium cellulosum So ce12. Within the cluster, sorF encodes a putative glycosyltransferase. To determine its function in sorangicin biosynthesis, SorF was heterologously expressed as a fusion protein in Escherichia coli. After purification by affinity chromatography, SorF was found to glucosylate sorangicin A in vitro, utilizing UDP-alpha-D-glucose as the natural donor substrate. Additionally, SorF showed high flexibility towards further UDP- and dTDP-sugars and was able to transfer several other sugar moieties-alpha-D-galactose, alpha-D-xylose, beta-L-rhamnose, and 6-deoxy-4-keto-alpha-D-glucose-onto the aglycon. SorF is therefore one of the rare glycosyltransferases able to transfer both D- and L-sugars, and could thus be used to generate novel sorangiosides.
authors.affiliation: Saarland University, Department of Pharmaceutical Biotechnology, P. O. Box 151150, 66041 Saarbrücken, Germany.
authors.forename: Maren
authors.initials: M
authors.lastname: Kopp
authors.forename: Carsten
authors.initials: C
authors.lastname: Rupprath
authors.forename: Herbert
authors.initials: H
authors.lastname: Irschik
authors.forename: Andreas
authors.initials: A
authors.lastname: Bechthold
authors.forename: Lothar
authors.initials: L
authors.lastname: Elling
authors.forename: Rolf
authors.initials: R
authors.lastname: Müller
mesh_terms: D001483:Base Sequence; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism*; D009231:Myxococcales / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D017931:DNA Primers; D016695:Glycosyltransferases