ArticleAntioxidants (Basel, Switzerland)2021
Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida.
Article in Antioxidants (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 21 citations in OpenAlex.
- The saltmarsh cordgrass Spartina anglica has novel genomic features that contribute to abiotic stress tolerance.Journal of experimental botany · 2026Article
- Genome-Wide Identification and Functional Studies of the APX Gene Family in Oat (Life (Basel, Switzerland) · 2026Article
- Article
- Effects of Monoterpene-Based Biostimulants on Chickpea (Biology · 2025Article
- Enhanced thermotolerance via overexpression of a stromal ascorbate peroxidase in Nannochloropsis oceanica.Plant cell reports · 2025Article
- APX2 Is an Ascorbate Peroxidase-Related Protein that Regulates the Levels of Plastocyanin in Chlamydomonas.Plant & cell physiology · 2024Article
- The ascorbate peroxidase-related protein: insights into its functioning in Chlamydomonas and Arabidopsis.Frontiers in plant science · 2024Review
- Ascorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin.Antioxidants (Basel, Switzerland) · 2023Article
- A sorghum ascorbate peroxidase with four binding sites has activity against ascorbate and phenylpropanoids.Plant physiology · 2023Article
- Four is better than one: Structure and function of a unique ascorbate peroxidase with four binding sites.Plant physiology · 2023Article
- Ascorbate-Glutathione Cycle Genes Families in Euphorbiaceae: Characterization and Evolutionary Analysis.Biology · 2022Article
- Discovering Diverse Roles of Peroxidases and Catalases in Photosynthetic and Non-Photosynthetic Eukaryotes.Antioxidants (Basel, Switzerland) · 2022Article
- Nitric Oxide (NO) Differentially Modulates the Ascorbate Peroxidase (APX) Isozymes of Sweet Pepper (Antioxidants (Basel, Switzerland) · 2022Article
- Genome-wide, evolutionary, and functional analyses of ascorbate peroxidase (APX) family in Poaceae species.Genetics and molecular biology · 2022Article
- Characterization of the Free and Membrane-Associated Fractions of the Thylakoid Lumen Proteome inInternational journal of molecular sciences · 2021Article
- Arabidopsis APx-R Is a Plastidial Ascorbate-Independent Peroxidase Regulated by Photomorphogenesis.Antioxidants (Basel, Switzerland) · 2021Article
- Evaluation of Peroxidase in Herbal Medicines Based on an Electrochemical Sensor.Frontiers in chemistry · 2021Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Ascorbate peroxidases (APX) are class I members of the Peroxidase-Catalase superfamily, a large group of evolutionarily related but rather divergent enzymes. Through mining in public databases, unusual subsets of APX homologs were identified, disclosing the existence of two yet uncharacterized families of peroxidases named ascorbate peroxidase-related (APX-R) and ascorbate peroxidase-like (APX-L). As APX, APX-R harbor all catalytic residues required for peroxidatic activity. Nevertheless, proteins of this family do not contain residues known to be critical for ascorbate binding and therefore cannot use it as an electron donor. On the other hand, APX-L proteins not only lack ascorbate-binding residues, but also every other residue known to be essential for peroxidase activity. Through a molecular phylogenetic analysis performed with sequences derived from basal Archaeplastida, the present study discloses the existence of hybrid proteins, which combine features of these three families. The results here presented show that the prevalence of hybrid proteins varies among distinct groups of organisms, accounting for up to 33% of total APX homologs in species of green algae. The analysis of this heterogeneous group of proteins sheds light on the origin of APX-R and APX-L and suggests the occurrence of a process characterized by the progressive deterioration of ascorbate-binding and catalytic sites towards neofunctionalization.
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