ArticleThe Plant cell2014
Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
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- Mapping multi-substrate specificity of Arabidopsis aminotransferases.Nature plants · 2025Article
- Maize big embryo 6 reveals roles of plastidial and cytosolic prephenate aminotransferases in seed and plant development.The Plant cell · 2025Article
- Aromatic Amino Acids: Exploring Microalgae as a Potential Biofactory.Biotech (Basel (Switzerland)) · 2025Review
- Evolution of aromatic amino acid metabolism in plants: a key driving force behind plant chemical diversity in aromatic natural products.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Plant terrestrialization: an environmental pull on the evolution of multi-sourced streptophyte phenolics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Multisubstrate specificity shaped the complex evolution of the aminotransferase family across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Metabolic engineering of Synechocystis sp. PCC 6803 for the improved production of phenylpropanoids.Microbial cell factories · 2024Article
- The cytosolic aminotransferase VAS1 coordinates aromatic amino acid biosynthesis and metabolism.Science advances · 2024Article
- Transcriptomic profiling analysis to identify genes associated with PA biosynthesis and insolubilization in the late stage of fruit development in C-PCNA persimmon.Scientific reports · 2022Article
- Using interdisciplinary, phylogeny-guided approaches to understand the evolution of plant metabolism.Plant molecular biology · 2022Review
- Harnessing evolutionary diversification of primary metabolism for plant synthetic biology.The Journal of biological chemistry · 2019Review
- Evolutionary Diversification of Primary Metabolism and Its Contribution to Plant Chemical Diversity.Frontiers in plant science · 2019Review
- RNA-Seq analysis reveals an essential role of tyrosine metabolism pathway in response to root-rot infection in Gerbera hybrida.PloS one · 2019Article
- Molecular basis of the evolution of alternative tyrosine biosynthetic routes in plants.Nature chemical biology · 2017Article
- Conserved Molecular Mechanism of TyrA Dehydrogenase Substrate Specificity Underlying Alternative Tyrosine Biosynthetic Pathways in Plants and Microbes.Frontiers in molecular biosciences · 2017Article
- Functional Annotations of Paralogs: A Blessing and a Curse.Life (Basel, Switzerland) · 2016Article
Corrections and comments
- Erratum issuedCORRECTION.2017
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aromatic amino acid Phe is required for protein synthesis and serves as the precursor of abundant phenylpropanoid plant natural products. While Phe is synthesized from prephenate exclusively via a phenylpyruvate intermediate in model microbes, the alternative pathway via arogenate is predominant in plant Phe biosynthesis. However, the molecular and biochemical evolution of the plant arogenate pathway is currently unknown. Here, we conducted phylogenetically informed biochemical characterization of prephenate aminotransferases (PPA-ATs) that belong to class-Ib aspartate aminotransferases (AspAT Ibs) and catalyze the first committed step of the arogenate pathway in plants. Plant PPA-ATs and succeeding arogenate dehydratases (ADTs) were found to be most closely related to homologs from Chlorobi/Bacteroidetes bacteria. The Chlorobium tepidum PPA-AT and ADT homologs indeed efficiently converted prephenate and arogenate into arogenate and Phe, respectively. A subset of AspAT Ib enzymes exhibiting PPA-AT activity was further identified from both Plantae and prokaryotes and, together with site-directed mutagenesis, showed that Thr-84 and Lys-169 play key roles in specific recognition of dicarboxylic keto (prephenate) and amino (aspartate) acid substrates. The results suggest that, along with ADT, a gene encoding prephenate-specific PPA-AT was transferred from a Chlorobi/Bacteroidetes ancestor to a eukaryotic ancestor of Plantae, allowing efficient Phe and phenylpropanoid production via arogenate in plants today.
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