ArticleScientific reports2017
Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD
Article in Scientific reports, 2017. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- Continuous Directed Evolution of a Short-Lived Plant Histidinol Dehydrogenase.ACS synthetic biology · 2026Article
- Interpretable prediction of zinc ion location in proteins with ZincSight.Protein science : a publication of the Protein Society · 2025Article
- Deciphering Functions of a Putative Histidinol Dehydrogenase in Acidovorax citrulli by Phenotypic and Proteomic Analyses.The plant pathology journal · 2025Article
- Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting.Frontiers in plant science · 2024Article
- Peroxisomal compartmentalization of amino acid biosynthesis reactions imposes an upper limit on compartment size.Nature communications · 2023Article
- Structural and mechanistic insights into the bifunctional HISN2 enzyme catalyzing the second and third steps of histidine biosynthesis in plants.Scientific reports · 2021Article
- The Role of Gene Elongation in the Evolution of Histidine Biosynthetic Genes.Microorganisms · 2020Article
- Chloroplastic Serine Hydroxymethyltransferase FromFrontiers in plant science · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Plants, lower eukaryotes, bacteria, and archaebacteria synthesise L-histidine (His) in a similar, multistep pathway that is absent in mammals. This makes the His biosynthetic route a promising target for herbicides, antifungal agents, and antibiotics. The last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histidinaldehyde to His. Over the course of the reaction, HDH utilises two molecules of NAD
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Registered trials
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