ArticlePloS one2014
Catalytic profile of Arabidopsis peroxidases, AtPrx-2, 25 and 71, contributing to stem lignification.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 58 citations in OpenAlex.
- Integrated omics reveal phenylpropanoid biosynthesis as a key defense pathway against Meloidogyne incognita in Cucumis metuliferus.BMC plant biology · 2026Article
- Genome-wide identification and expression analysis of the class III peroxidase gene family in Medicago sativa.BMC plant biology · 2025Article
- AtPrx71-mediated regulation of stem elongation, gravitropic response, and IAA accumulation in Arabidopsis.Planta · 2025Article
- Heterologous expression of Arabidopsis laccase2, laccase4 and peroxidase52 driven under developing xylem specific promoter DX15 improves saccharification in populus.Biotechnology for biofuels and bioproducts · 2024Article
- VAMP726 from maize and Arabidopsis confers pollen resistance to heat and UV radiation by influencing lignin content of sporopollenin.Plant communications · 2023Article
- Modulation of lignin biosynthesis for drought tolerance in plants.Frontiers in plant science · 2023Review
- Reduced Expression ofPlants (Basel, Switzerland) · 2022Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2022Article
- Class III Peroxidases in Response to Multiple Abiotic Stresses inInternational journal of molecular sciences · 2022Article
- Resequencing of 301 ramie accessions identifies genetic loci and breeding selection for fibre yield traits.Plant biotechnology journal · 2022Article
- Comparative transcriptome analysis reveals key pathways and genes involved in trichome development in tea plant (Frontiers in plant science · 2022Article
- Integrative small RNA and transcriptome analysis provides insight into key role of miR408 towards drought tolerance response in cowpea.Plant cell reports · 2022Article
- Global transcriptome and coexpression network analyses reveal cultivar-specific molecular signatures associated with different rooting depth responses to drought stress in potato.Frontiers in plant science · 2022Article
- Article
- Phenoloxidases in Plants-How Structural Diversity Enables Functional Specificity.Frontiers in plant science · 2021Review
- Extensins: Self-Assembly, Crosslinking, and the Role of Peroxidases.Frontiers in plant science · 2021Review
- Laccases and Peroxidases Co-Localize in Lignified Secondary Cell Walls throughout Stem Development.Plant physiology · 2020Article
- Phenylpropanoids Are Connected to Cell Wall Fortification and Stress Tolerance in Avocado Somatic Embryogenesis.International journal of molecular sciences · 2020Article
- Scalable High-Performance Production of Recombinant Horseradish Peroxidase fromInternational journal of molecular sciences · 2020Article
- Comparative transcriptome analysis of galls from four different host plants suggests the molecular mechanism of gall development.PloS one · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignins are aromatic heteropolymers that arise from oxidative coupling of lignin precursors, including lignin monomers (p-coumaryl, coniferyl, and sinapyl alcohols), oligomers, and polymers. Whereas plant peroxidases have been shown to catalyze oxidative coupling of monolignols, the oxidation activity of well-studied plant peroxidases, such as horseradish peroxidase C (HRP-C) and AtPrx53, are quite low for sinapyl alcohol. This characteristic difference has led to controversy regarding the oxidation mechanism of sinapyl alcohol and lignin oligomers and polymers by plant peroxidases. The present study explored the oxidation activities of three plant peroxidases, AtPrx2, AtPrx25, and AtPrx71, which have been already shown to be involved in lignification in the Arabidopsis stem. Recombinant proteins of these peroxidases (rAtPrxs) were produced in Escherichia coli as inclusion bodies and successfully refolded to yield their active forms. rAtPrx2, rAtPrx25, and rAtPrx71 were found to oxidize two syringyl compounds (2,6-dimethoxyphenol and syringaldazine), which were employed here as model monolignol compounds, with higher specific activities than HRP-C and rAtPrx53. Interestingly, rAtPrx2 and rAtPrx71 oxidized syringyl compounds more efficiently than guaiacol. Moreover, assays with ferrocytochrome c as a substrate showed that AtPrx2, AtPrx25, and AtPrx71 possessed the ability to oxidize large molecules. This characteristic may originate in a protein radical. These results suggest that the plant peroxidases responsible for lignin polymerization are able to directly oxidize all lignin precursors.
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