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Isoprenoid phosphonophosphates as glycosyltransferase acceptor substrates.

ABSTRACT: Glycosyltransferases that act on polyprenol pyrophosphate substrates are challenging to study because their lipid-linked substrates are difficult to isolate from natural sources and arduous to synthesize. To facilitate access to glycosyl acceptors, we assembled phosphonophosphate analogues and showed these are effective substrate surrogates for GlfT1, the essential product of mycobacterial gene Rv3782. Under chemically defined conditions, the galactofuranosyltransferase GlfT1 catalyzes the formation of a tetrasaccharide sequence en route to assembly of the mycobacterial galactan.

SUBMITTER: Martinez Farias MA

PROVIDER: S-EPMC4073833 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Isoprenoid phosphonophosphates as glycosyltransferase acceptor substrates.

Martinez Farias Mario A MA Kincaid Virginia A VA Annamalai Venkatachalam R VR Kiessling Laura L LL

Journal of the American Chemical Society 20140610 24

Glycosyltransferases that act on polyprenol pyrophosphate substrates are challenging to study because their lipid-linked substrates are difficult to isolate from natural sources and arduous to synthesize. To facilitate access to glycosyl acceptors, we assembled phosphonophosphate analogues and showed these are effective substrate surrogates for GlfT1, the essential product of mycobacterial gene Rv3782. Under chemically defined conditions, the galactofuranosyltransferase GlfT1 catalyzes the forma ...[more]

PMID: 24866828

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