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Enzymatic synthesis of 3-deoxy-d-manno-octulosonic acid (KDO) and its application for LPS assembly.

ABSTRACT: The studies of 3-deoxy-d-manno-octulosonic acid (KDO) have been hindered due to its limited availability. Herein, an efficient enzymatic system for the facile synthesis of KDO from easy-to-get starting materials is described. In this one-pot three-enzyme (OPME) system, d-ribulose 5-phosphate, which was prepared from d-xylose, was employed as starting materials. The reaction process involves the isomerization of d-ribulose 5-phosphate to d-arabinose 5-phosphate catalyzed by d-arabinose 5-phosphate isomerase (KdsD), the aldol condensation of d-arabinose 5-phosphate and phosphoenolpyruvate (PEP) catalyzed by KDO 8-phosphate synthetase (KdsA), and the hydrolysis of KDO-8-phosphate catalyzed by KDO 8-phosphate phosphatase (KdsC). By using this OPME system, 72% isolated yield was obtained. The obtained KDO was further transferred to lipid A by KDO transferase from Escherichia coli (WaaA).

SUBMITTER: Wen L

PROVIDER: S-EPMC5972366 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Enzymatic synthesis of 3-deoxy-d-manno-octulosonic acid (KDO) and its application for LPS assembly.

Wen Liuqing L Zheng Yuan Y Li Tiehai T Wang Peng George PG

Bioorganic & medicinal chemistry letters 20160421 12

The studies of 3-deoxy-d-manno-octulosonic acid (KDO) have been hindered due to its limited availability. Herein, an efficient enzymatic system for the facile synthesis of KDO from easy-to-get starting materials is described. In this one-pot three-enzyme (OPME) system, d-ribulose 5-phosphate, which was prepared from d-xylose, was employed as starting materials. The reaction process involves the isomerization of d-ribulose 5-phosphate to d-arabinose 5-phosphate catalyzed by d-arabinose 5-phosphat ...[more]

PMID: 27173798

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Lipopolysaccharide 3-deoxy-D-manno-octulosonic acid (Kdo) core determines bacterial association of secreted toxins.

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Identification of phosphorylated 3-deoxy-manno-octulosonic acid as a component of Haemophilus influenzae lipopolysaccharide.

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Project description:The 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase gene of Legionella pneumophila was cloned and sequenced. Despite remarkable structural differences in lipid A, the gene complemented a corresponding Escherichia coli mutant and was shown to encode a bifunctional enzyme which transferred 2 Kdo residues to a lipid A acceptor of E. coli.

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Natural selection in the chicken host identifies 3-deoxy-D-manno-octulosonic acid kinase residues essential for phosphorylation of Pasteurella multocida lipopolysaccharide.

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| S-EPMC2937434 | biostudies-literature

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