title: Isoprenoid phosphonophosphates as glycosyltransferase acceptor substrates.
abstract: Glycosyltransferases that act on polyprenol pyrophosphate substrates are challenging to study because their lipid-linked substrates are difficult to isolate from natural sources and arduous to synthesize. To facilitate access to glycosyl acceptors, we assembled phosphonophosphate analogues and showed these are effective substrate surrogates for GlfT1, the essential product of mycobacterial gene Rv3782. Under chemically defined conditions, the galactofuranosyltransferase GlfT1 catalyzes the formation of a tetrasaccharide sequence en route to assembly of the mycobacterial galactan.
authors.affiliation: Department of Chemistry and ‡Department of Biochemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
authors.forename: Mario A
authors.initials: MA
authors.lastname: Martinez Farias
authors.forename: Virginia A
authors.initials: VA
authors.lastname: Kincaid
authors.forename: Venkatachalam R
authors.initials: VR
authors.lastname: Annamalai
authors.forename: Laura L
authors.initials: LL
authors.lastname: Kiessling
mesh_terms: D055162:Biocatalysis; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D011106:Polyisoprenyl Phosphates / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011106:Polyisoprenyl Phosphates; D016695:Glycosyltransferases