title: Total synthesis of polyprenyl N-glycolyl lipid II as a mycobacterial transglycosylase substrate.
abstract: A feasible synthetic approach toward the Mycobacterium tuberculosis (Mtb) N-glycolyl lipid II-like molecule 1 is described. Compound 1 bears pendant undecaprenol and l-lysin moieties instead of the naturally occurring decaprenol and meso-diaminopimelic acid, which are not readily available. Functionalization of 1 with a fluorophore on the peptide side chain gave 14, which was found to be recognized as an Mtb TGase substrate. This result suggests it has tremendous utility for mechanistic studies, the characterization of mycobacterial enzymes, and mycobacterial TGase inhibitor evaluation.
authors.affiliation: The Genomics Research Center, Academia Sinica, Nankang, Taipei, Taiwan.
authors.forename: Fan-Chun
authors.initials: FC
authors.lastname: Meng
authors.forename: Kuo-Ting
authors.initials: KT
authors.lastname: Chen
authors.forename: Lin-Ya
authors.initials: LY
authors.lastname: Huang
authors.forename: Hao-Wei
authors.initials: HW
authors.lastname: Shih
authors.forename: Han-Hui
authors.initials: HH
authors.lastname: Chang
authors.forename: Fu-Yao
authors.initials: FY
authors.lastname: Nien
authors.forename: Pi-Hui
authors.initials: PH
authors.lastname: Liang
authors.forename: Ting-Jen R
authors.initials: TJ
authors.lastname: Cheng
authors.forename: Chi-Huey
authors.initials: CH
authors.lastname: Wong
authors.forename: Wei-Chieh
authors.initials: WC
authors.lastname: Cheng
mesh_terms: D006017:Glycolipids / Q000737:chemistry* / Q000378:metabolism*; D016695:Glycosyltransferases / Q000378:metabolism; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D006017:Glycolipids; D016695:Glycosyltransferases