ArticleNature plants2025
Mapping multi-substrate specificity of Arabidopsis aminotransferases.
Article in Nature plants, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- AspAT orchestrates metabolic and transcriptional networks for drought adaptation in poplar.Journal of plant research · 2026Article
- Transaminases engineering and their cascade systems for natural product synthesis.Applied biochemistry and biotechnology · 2026Review
- A plastoglobuli-localized enzyme links phenylalanine biosynthesis to translational homeostasis in maize.Nature communications · 2026Article
- Sulfate starvation response modules connect sulfur metabolism to photorespiration and photosynthesis.The Plant journal : for cell and molecular biology · 2026Article
- Amino Acids as Multifunctional Molecules in Plants: From Fundamental Metabolism to Precision Agriculture.Plants (Basel, Switzerland) · 2026Review
- High-throughput screening for biostimulant discovery: opportunities to enhance nitrogen use efficiency.Frontiers in plant science · 2026Review
- Stress Adaptation Phenomena ofPlants (Basel, Switzerland) · 2025Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Nitrogen is an essential element in all organisms, and its availability and use efficiency directly impact organismal growth and performance, especially in plants. Aminotransferases are core enzymes of the nitrogen metabolic network for synthesizing various organonitrogen compounds. Although each aminotransferase can potentially catalyse hundreds of transamination reactions with different combinations of amino and keto acid substrates, the full functionality of many aminotransferases remains elusive. Here we employed high-throughput gene synthesis and enzyme assay platforms to determine the substrate specificities of 38 aminotransferases of Arabidopsis thaliana and unveiled many previously unrecognized activities among a total of 4,104 reactions tested. The integration of these biochemical data in an enzyme-constrained metabolic model of Arabidopsis and in silico simulation further revealed that the promiscuity of aminotransferases may alter nitrogen distribution profiles and contribute to the robustness of the nitrogen metabolic network. This study provides foundational knowledge for deciphering the plant nitrogen metabolic network and improving nitrogen use efficiency in crops.
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Registered trials
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