ArticlePlanta2022
The first step into phenolic metabolism in the hornwort Anthoceros agrestis: molecular and biochemical characterization of two phenylalanine ammonia-lyase isoforms.
Article in Planta, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Early occurrence of caffeoylshikimic acid esterase (CSE) activity in the hornwort Anthoceros agrestis.Planta · 2026Article
- Phenylalanine Ammonia-Lyase: A Core Regulator of Plant Carbon Metabolic Flux Redistribution-From Molecular Mechanisms and Growth Modulation to Stress Adaptability.Plants (Basel, Switzerland) · 2025Review
- Evolutionary analysis of anthocyanin biosynthetic genes: insights into abiotic stress adaptation.Plant molecular biology · 2024Review
- Integrated transcriptomics and metabolomics provide insights into the biosynthesis of militarine in the cell suspension culture system of Bletilla striata.Advanced biotechnology · 2024Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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Abstract
MAIN
conclusionTwo isoforms of phenylalanine ammonia-lyase (PAL) have been isolated as cDNA sequences from the hornwort Anthoceros agrestis. The encoded enzymes convert L-phenylalanine and to lower extents L-tyrosine and L-histidine. Thus, the functional presence of the general phenylpropanoid pathway in one of the earliest land plant groups is established. The hornwort Anthoceros agrestis has an elaborated phenolic metabolism resulting in phenolic compounds, such as rosmarinic acid or megacerotonic acid. The general phenylpropanoid pathway is involved in the biosynthesis of these compounds. Two phenylalanine ammonia-lyase (PAL) genes, AaPAL1 and AaPAL2, have been identified in Anthoceros agrestis and the protein with an N-terminal 6xHis-tag heterologously synthesized in Escherichia coli for a full biochemical characterization. Both PAL proteins accept L-phenylalanine, L-tyrosine as well as L-histidine as substrates, although the activity is explicitly the highest with L-phenylalanine. K
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