ArticleJournal of experimental botany2023
Metabolic link between auxin production and specialized metabolites in Sorghum bicolor.
Article in Journal of experimental botany, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Aldoximes serve as auxin precursors and repress phenylpropanoid metabolism in tomato.bioRxiv : the preprint server for biology · 2026Article
- The CYP71A, NIT, AMI, and IAMH gene families are dispensable for indole-3-acetaldoxime-mediated auxin biosynthesis in Arabidopsis.The Plant cell · 2025Article
- Genome analysis and hyphal movement characterization of the hitchhiker endohyphalApplied and environmental microbiology · 2024Article
- Altered methionine metabolism impacts phenylpropanoid production and plant development in Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2023Article
- Occurrence, Function, and Biosynthesis of the Natural Auxin Phenylacetic Acid (PAA) in Plants.Plants (Basel, Switzerland) · 2023Review
- Amino acid substrate specificities and tissue expression profiles of the nine CYP79A encoding genes in Sorghum bicolor.Physiologia plantarumArticle
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Authors and funding
9 authors at 2 institutions in 1 country.
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Abstract
Aldoximes are amino acid derivatives that serve as intermediates for numerous specialized metabolites including cyanogenic glycosides, glucosinolates, and auxins. Aldoxime formation is mainly catalyzed by cytochrome P450 monooxygenases of the 79 family (CYP79s) that can have broad or narrow substrate specificity. Except for SbCYP79A1, aldoxime biosynthetic enzymes in the cereal sorghum (Sorghum bicolor) have not been characterized. This study identified nine CYP79-encoding genes in the genome of sorghum. A phylogenetic analysis of CYP79 showed that SbCYP79A61 formed a subclade with maize ZmCYP79A61, previously characterized to be involved in aldoxime biosynthesis. Functional characterization of this sorghum enzyme using transient expression in Nicotiana benthamiana and stable overexpression in Arabidopsis thaliana revealed that SbCYP79A61 catalyzes the production of phenylacetaldoxime (PAOx) from phenylalanine but, unlike the maize enzyme, displays no detectable activity against tryptophan. Additionally, targeted metabolite analysis after stable isotope feeding assays revealed that PAOx can serve as a precursor of phenylacetic acid (PAA) in sorghum and identified benzyl cyanide as an intermediate of PAOx-derived PAA biosynthesis in both sorghum and maize. Taken together, our results demonstrate that SbCYP79A61 produces PAOx in sorghum and may serve in the biosynthesis of other nitrogen-containing phenylalanine-derived metabolites involved in mediating biotic and abiotic stresses.
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