ArticleScience China. Life sciences2022
A conservative distribution of tridomain NDP-heptose synthetases in actinobacteria.
Article in Science China. Life sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- NDP-β-d-manno-heptoses are small molecule agonists sensed by the vertebrates to discriminate organisms of different kingdoms.Clinical and translational medicine · 2024Article
- The Biotransformation and Influence on the Functional Activities of Metabolites during the Fermentation ofFoods (Basel, Switzerland) · 2024Article
- Characterization of the ADP-β-D-manno-heptose biosynthetic enzymes from two pathogenic Vibrio strains.Applied microbiology and biotechnology · 2024Article
- Insights into the biosynthesis of septacidin l-heptosamine moiety unveils a VOC family sugar epimerase.Acta pharmaceutica Sinica. B · 2023Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heptoses are important structural components of Gram-negative bacterium cell wall and participate in bacterial colonization, infection, and immune recognition. Current knowledge of NDP-heptose originating from D-sedoheptulose 7-phosphate in Grampositive bacterium remains limited. Here, in silico analysis suggested that the special tridomain NDP-heptose synthetases with isomerase, kinase, and nucleotidyltransferase activities are conservatively distributed in Actinobacteria class of Gram-positive bacterium. Enzymatical characterization of the tridomain proteins from different strains showed that they are involved in ADP-D-glycero-β-D-manno-heptose biosynthesis despite the unexpected discovery of kinase activities deficient in some proteins. The presence of three types of NDP-heptose synthetases in Gram-positive bacterium suggests that it is also a rich source of heptoses and the heptose moieties may play important roles in vivo. Our work updates the understanding of NDP-heptose biosynthesis in Gram-positive bacterium and lays a solid foundation for further physiological function explorations.
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