ArticleNature communications2024
Substrate binding and catalytic mechanism of the Se-glycosyltransferase SenB in the biosynthesis of selenoneine.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Emerging tools to investigate the contribution of selenium to ferroptosis and beyond.Nature chemical biology · 2026Review
- Comparative study of two xanthan gum glycosyltransferases combining AI structure predictions and molecular modeling.bioRxiv : the preprint server for biology · 2026Article
- Selenoneine, a food chain component with potential neuroprotective effects against electrophilic mercury forms.Advances in neurotoxicology · 2026Article
- Computational characterization of the xanthan gum glycosyltransferase GumK.PLoS computational biology · 2025Article
- Structural analysis of the tetrahydrobiopterin glucosyltransferase PsBGluT from Pseudanabaena sp. Chao 1811.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Semirational Design of SenC to Enhance Organic Selenium Biosynthesis.Microbial biotechnology · 2025Article
- 50 Years of Organoselenium Chemistry, Biochemistry and Reactivity: Mechanistic Understanding, Successful and Controversial Stories.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Structures of SenB and SenA enzymes fromHeliyon · 2024Article
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Authors and funding
7 authors.
Funding
Abstract
Selenium is an essential multifunctional trace element in diverse organisms. The only Se-glycosyltransferase identified that catalyzes the incorporation of selenium in selenoneine biosynthesis is SenB from Variovorax paradoxus. Although the biochemical function of SenB has been investigated, its substrate specificity, structure, and catalytic mechanism have not been elucidated. Here, we reveal that SenB exhibits sugar donor promiscuity and can utilize six UDP-sugars to generate selenosugars. We report crystal structures of SenB complexed with different UDP-sugars. The key elements N20/T23/E231 contribute to the sugar donor selectivity of SenB. A proposed catalytic mechanism is tested by structure-guided mutagenesis, revealing that SenB yields selenosugars by forming C-Se glycosidic bonds via spontaneous deprotonation and disrupting Se-P bonds by nucleophilic water attack, which is initiated by the critical residue K158. Furthermore, we functionally and structurally characterize two other Se-glycosyltransferases, CbSenB from Comamonadaceae bacterium and RsSenB from Ramlibacter sp., which also exhibit sugar donor promiscuity.
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