ArticleBioorganic & medicinal chemistry letters2016
Enzymatic synthesis of 3-deoxy-d-manno-octulosonic acid (KDO) and its application for LPS assembly.
Article in Bioorganic & medicinal chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
- Proteome-Wide Reverse Vaccinology and Immunoinformatics-Guided Design of a Multi-Epitope Vaccine AgainstInternational journal of molecular sciences · 2026Article
- Comparative glycomic analysis of Mimiviridae and Marseilleviridae uncovers host-related and lineage-specific glycosylation.Journal of biochemistry · 2026Article
- Putative rhamnogalacturonan-II glycosyltransferase identified through callus gene editing which bypasses embryo lethality.Plant physiology · 2024Article
- Chemical Reporters for Bacterial Glycans: Development and Applications.Chemical reviews · 2022Review
- Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.International journal of molecular sciences · 2019Review
- Design, synthesis, and structural elucidation of novel NmeNANAS inhibitors for the treatment of meningococcal infection.PloS one · 2019Article
- Two-step enzymatic synthesis of 6-deoxy-L-psicose.Tetrahedron letters · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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).
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