ArticleThe Journal of biological chemistry2014
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- 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
- Transposon sequencing reveals metabolic pathways essential for Mycobacterium tuberculosis infection.PLoS pathogens · 2024Article
- Metabolic engineering of Synechocystis sp. PCC 6803 for the improved production of phenylpropanoids.Microbial cell factories · 2024Article
- Occurrence, Function, and Biosynthesis of the Natural Auxin Phenylacetic Acid (PAA) in Plants.Plants (Basel, Switzerland) · 2023Review
- New Insight into Aspartate Metabolic Pathways inInternational journal of molecular sciences · 2022Article
- Harnessing evolutionary diversification of primary metabolism for plant synthetic biology.The Journal of biological chemistry · 2019Review
- Genome-Based Metabolic Reconstruction Unravels the Key Role of B12 in Methionine Auxotrophy of anFrontiers in microbiology · 2019Article
- Evolutionary Diversification of Primary Metabolism and Its Contribution to Plant Chemical Diversity.Frontiers in plant science · 2019Review
- Conserved Molecular Mechanism of TyrA Dehydrogenase Substrate Specificity Underlying Alternative Tyrosine Biosynthetic Pathways in Plants and Microbes.Frontiers in molecular biosciences · 2017Article
- Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.The Plant cell · 2014Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aromatic amino acids phenylalanine and tyrosine represent essential sources of high value natural aromatic compounds for human health and industry. Depending on the organism, alternative routes exist for their synthesis. Phenylalanine and tyrosine are synthesized either via phenylpyruvate/4-hydroxyphenylpyruvate or via arogenate. In arogenate-competent microorganisms, an aminotransferase is required for the transamination of prephenate into arogenate, but the identity of the genes is still unknown. We present here the first identification of prephenate aminotransferases (PATs) in seven arogenate-competent microorganisms and the discovery that PAT activity is provided by three different classes of aminotransferase, which belong to two different fold types of pyridoxal phosphate enzymes: an aspartate aminotransferase subgroup 1β in tested α- and β-proteobacteria, a branched-chain aminotransferase in tested cyanobacteria, and an N-succinyldiaminopimelate aminotransferase in tested actinobacteria and in the β-proteobacterium Nitrosomonas europaea. Recombinant PAT enzymes exhibit high activity toward prephenate, indicating that the corresponding genes encode bona fide PAT. PAT functionality was acquired without other modification of substrate specificity and is not a general catalytic property of the three classes of aminotransferases.
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