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Synthesis of lipid-linked arabinofuranose donors for glycosyltransferases.

ABSTRACT: Mycobacteria and corynebacteria use decaprenylphosphoryl-?-D-arabinofuranose (DPA) as a critical cell wall building block. Arabinofuranosyltransferases that process this substrate to mediate cell wall assembly have served as drug targets, but little is known about the substrate specificity of any of these enzymes. To probe substrate recognition of DPA, we developed a general and efficient synthetic route to ?-D-arabinofuranosyl phosphodiesters. In this approach, the key glycosyl phosphodiester bond-forming reaction proceeds with high ?-selectivity. In addition to its stereoselectivity, our route provides the means to readily access a variety of different lipid analogues, including aliphatic and polyprenyl substrates.

SUBMITTER: Kraft MB

PROVIDER: S-EPMC3646515 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Synthesis of lipid-linked arabinofuranose donors for glycosyltransferases.

Kraft Matthew B MB Martinez Farias Mario A MA Kiessling Laura L LL

The Journal of organic chemistry 20130207 5

Mycobacteria and corynebacteria use decaprenylphosphoryl-β-D-arabinofuranose (DPA) as a critical cell wall building block. Arabinofuranosyltransferases that process this substrate to mediate cell wall assembly have served as drug targets, but little is known about the substrate specificity of any of these enzymes. To probe substrate recognition of DPA, we developed a general and efficient synthetic route to β-D-arabinofuranosyl phosphodiesters. In this approach, the key glycosyl phosphodiester b ...[more]

PMID: 23373821

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