Total synthesis of polyprenyl N-Glycolyl Lipid II as a mycobacterial transglycosylase substrate
Journal
Organic Letters
Journal Volume
13
Journal Issue
19
Pages
5306-5309
Date Issued
2011
Author(s)
Chen K.-T.
Huang L.-Y.
Shih H.-W.
Chang H.-H.
Nien F.-Y.
Cheng T.-J. R.
Wong C.-H.
Cheng W.-C.
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. ? 2011 American Chemical Society.
SDGs
Other Subjects
glycolipid; glycosyltransferase; article; chemistry; enzyme specificity; metabolism; Mycobacterium tuberculosis; Glycolipids; Glycosyltransferases; Mycobacterium tuberculosis; Substrate Specificity
Type
journal article