ArticleACS chemical biology2016
Identification of a Novel Mycobacterial Arabinosyltransferase Activity Which Adds an Arabinosyl Residue to α-d-Mannosyl Residues.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- A new role for lipoproteins LpqZ and FecB in orchestrating mycobacterial cell envelope biogenesis.mBio · 2026Article
- Structure and Function of Mycobacterial Arabinofuranosyltransferases.Sub-cellular biochemistry · 2022Article
- Antibiotics and resistance: the two-sided coin of the mycobacterial cell wall.Cell surface (Amsterdam, Netherlands) · 2020Review
- The thick waxy coat of mycobacteria, a protective layer against antibiotics and the host's immune system.The Biochemical journal · 2020Review
- Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.Molecular cell · 2020Article
- Secondary Extended Mannan Side Chains and Attachment of the Arabinan in Mycobacterial Lipoarabinomannan.Communications chemistry · 2020Article
- Cloning and Partial Characterization of an Endo-α-(1→6)-d-Mannanase Gene fromInternational journal of molecular sciences · 2019Article
- Characterization of Arabinosyl Transfer Reactions in the Biosynthesis of Mycobacterial Cell Envelope (Lipo)Polysaccharides.Methods in molecular biology (Clifton, N.J.) · 2019Article
- The singularCell surface (Amsterdam, Netherlands) · 2018Article
- Disruption of Mycobacterial AftB Results in Complete Loss of Terminal β(1 → 2) Arabinofuranose Residues of Lipoarabinomannan.ACS chemical biology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The arabinosyltransferases responsible for the biosynthesis of the arabinan domains of two abundant heteropolysaccharides of the cell envelope of all mycobacterial species, lipoarabinomannan and arabinogalactan, are validated drug targets. Using a cell envelope preparation from Mycobacterium smegmatis as the enzyme source and di- and trimannoside synthetic acceptors, we uncovered a previously undetected arabinosyltransferase activity. Thin layer chromatography, GC/MS, and LC/MS/MS analyses of the major enzymatic product are consistent with the transfer of an arabinose residue to the 6 position of the terminal mannosyl residue at the nonreducing end of the acceptors. The newly identified enzymatic activity is resistant to ethambutol and could correspond to the priming arabinosyl transfer reaction that occurs during lipoarabinomannan biosynthesis.
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Registered trials
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