ArticlePloS one2013
Molecular evolution of threonine dehydratase in bacteria.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Trans-interface coupling in the tetrameric enzyme underlies allosteric control inJournal of structural biology: X · 2026Article
- High side chain promiscuity of the terminal enzyme in the homologation pathway for l-phenylalanine and l-tyrosine.bioRxiv : the preprint server for biology · 2026Article
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- Impact of trace metal supplementation on anaerobic biological methanation under hydrogen and carbon dioxide starvation.NPJ biofilms and microbiomes · 2025Article
- How to identify cell material in a single ice grain emitted from Enceladus or Europa.Science advances · 2024Article
- FK506-binding protein, FKBP12, promotes serine utilization and negatively regulates threonine deaminase in fission yeast.iScience · 2022Article
- The σRNA biology · 2019Article
- Molecular evolution of acetohydroxyacid synthase in bacteria.MicrobiologyOpen · 2017Article
- Generation of mutant threonine dehydratase and its effects on isoleucine synthesis in Corynebacterium glutamicum.World journal of microbiology & biotechnology · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Threonine dehydratase converts L-threonine to 2-ketobutyrate. Several threonine dehydratases exist in bacteria, but their origins and evolutionary pathway are unknown. Here we analyzed all the available threonine dehydratases in bacteria and proposed an evolutionary pathway leading to the genes encoding three different threonine dehydratases CTD, BTD1 and BTD2. The ancestral threonine dehydratase might contain only a catalytic domain, but one or two ACT-like subdomains were fused during the evolution, resulting BTD1 and BTD2, respectively. Horizontal gene transfer, gene fusion, gene duplication, and gene deletion may occur during the evolution of this enzyme. The results are important for understanding the functions of various threonine dehydratases found in bacteria.
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Registered trials
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