Rapid preparation of mycobacterium N-glycolyl lipid i and lipid II derivatives: A biocatalytic approach
Journal
Chemistry - A European Journal
Journal Volume
19
Journal Issue
3
Pages
834-838
Date Issued
2013
Author(s)
Abstract
Breaking down barriers: A rapid, inexpensive preparation of the structurally complex mycobacterial N-glycolyl LipidI, LipidII, and their analogues from a range of different synthetic N-glycolyl and N-glycinyl Park's nucleotides is described (see scheme). The biotransformations were catalyzed by a readily available biocatalyst obtained from a bacterial cell-free membrane fraction. The unnatural N-glycinyl LipidII was found to be a substrate of Mycobacterium tuberculosis (Mtb) transglycosylase, PonA, and N-glycolyl LipidI was a weak inhibitor against PonA. Copyright ? 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Subjects
antibiotics; biocatalysis; inhibitors; synthetic methods; transglycosylase
SDGs
Other Subjects
Biocatalysis; Cell-free; Membrane fraction; Mycobacterial; Mycobacterium tuberculosis; Synthetic methods; transglycosylase; Antibiotics; Corrosion inhibitors; Synthesis (chemical); Chemistry; bacterial protein; glycolipid; mraY protein, Bacteria; n acetylglucosaminyltransferase; outer membrane protein; transferase; UDP N acetylglucosamine N acetylmuramyl (pentapeptide)pyrophosphoryl undecaprenol N acetylglucosamine transferase; UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase; article; biocatalysis; biosynthesis; chemical structure; chemistry; enzymology; metabolism; Mycobacterium tuberculosis; Bacterial Outer Membrane Proteins; Bacterial Proteins; Biocatalysis; Glycolipids; Molecular Structure; Mycobacterium tuberculosis; N-Acetylglucosaminyltransferases; Transferases
Type
journal article