Abstract
Breaking down barriers: A rapid, inexpensive preparation of the structurally complex mycobacterial N-glycolyl Lipid I, Lipid II, 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 Lipid II was found to be a substrate of Mycobacterium tuberculosis (Mtb) transglycosylase, PonA, and N-glycolyl Lipid I was a weak inhibitor against PonA.
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Outer Membrane Proteins / metabolism*
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Bacterial Proteins / metabolism*
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Biocatalysis
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Glycolipids / biosynthesis*
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Glycolipids / chemistry
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Glycolipids / metabolism
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Molecular Structure
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Mycobacterium tuberculosis / chemistry*
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Mycobacterium tuberculosis / enzymology
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Mycobacterium tuberculosis / metabolism
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N-Acetylglucosaminyltransferases / metabolism*
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Transferases (Other Substituted Phosphate Groups)
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Transferases / metabolism*
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Glycolipids
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Transferases
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N-Acetylglucosaminyltransferases
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UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
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Transferases (Other Substituted Phosphate Groups)
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mraY protein, Bacteria