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Identification of a Novel Mycobacterial Arabinosyltransferase Activity Which Adds an Arabinosyl Residue to α-d-Mannosyl Residues.

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.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Angala SK,McNeil MR,Zou L,Liav A,Zhang J,Lowary TL,Jackson M

doi

10.1021/acschembio.6b00093

subject

Has Abstract

pub_date

2016-06-17 00:00:00

pages

1518-24

issue

6

eissn

1554-8929

issn

1554-8937

journal_volume

11

pub_type

杂志文章

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