ArticleScientific reports2021
Structural and mechanistic insights into the bifunctional HISN2 enzyme catalyzing the second and third steps of histidine biosynthesis in plants.
Article in Scientific reports, 2021. 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.
- Drought Stress Mediated Changes in Food Crops: Mechanisms and Remediation Strategies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Histidinol dehydrogenase (HisD): a critical regulator ofMicrobiology spectrum · 2026Article
- Histidine limitation alters plant development and influences the TOR network.Journal of experimental botany · 2025Article
- Multi-omics analysis reveals genetic architecture and local adaptation of coumarins metabolites in Populus.BMC plant biology · 2024Article
- Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting.Frontiers in plant science · 2024Article
- Catalytic Cycle of the Bifunctional Enzyme Phosphoribosyl-ATP Pyrophosphohydrolase/Phosphoribosyl-AMP Cyclohydrolase.ACS catalysis · 2023Article
- Deciphering the structure ofComputational and structural biotechnology journal · 2022Article
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3 authors.
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Abstract
The second and third steps of the histidine biosynthetic pathway (HBP) in plants are catalyzed by a bifunctional enzyme-HISN2. The enzyme consists of two distinct domains, active respectively as a phosphoribosyl-AMP cyclohydrolase (PRA-CH) and phosphoribosyl-ATP pyrophosphatase (PRA-PH). The domains are analogous to single-domain enzymes encoded by bacterial hisI and hisE genes, respectively. The calculated sequence similarity networks between HISN2 analogs from prokaryotes and eukaryotes suggest that the plant enzymes are closest relatives of those in the class of Deltaproteobacteria. In this work, we obtained crystal structures of HISN2 enzyme from Medicago truncatula (MtHISN2) and described its architecture and interactions with AMP. The AMP molecule bound to the PRA-PH domain shows positioning of the N1-phosphoribosyl relevant to catalysis. AMP bound to the PRA-CH domain mimics a part of the substrate, giving insights into the reaction mechanism. The latter interaction also arises as a possible second-tier regulatory mechanism of the HBP flux, as indicated by inhibition assays and isothermal titration calorimetry.
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