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Article

Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida

1
Centro de Biotecnologia, Programa de Pós-Graduação em Biologia Celular e Molecular, Universidade Federal do Rio Grande do Sul, Porto Alegre 91509-900, Brazil
2
Departamento de Botânica, Instituto de Ciências Biológicas, Universidade Federal De Minas Gerais, Belo Horizonte 31270-901, Brazil
3
Laboratory of Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, SK-84551 Bratislava, Slovakia
4
Programa de Pós-Graduação em Genética e Biologia Molecular, Departamento de Genética, Universidade Federal do Rio Grande do Sul, Porto Alegre 91509-900, Brazil
*
Author to whom correspondence should be addressed.
Academic Editors: Simone Carradori and Francisco J. Corpas
Antioxidants 2021, 10(4), 597; https://doi.org/10.3390/antiox10040597
Received: 1 March 2021 / Revised: 9 April 2021 / Accepted: 10 April 2021 / Published: 13 April 2021
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. View Full-Text
Keywords: ascorbate peroxidase—APX; APX-R; APX-L; catalytic sites; substrate; protein divergence ascorbate peroxidase—APX; APX-R; APX-L; catalytic sites; substrate; protein divergence
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MDPI and ACS Style

Lazzarotto, F.; Menguer, P.K.; Del-Bem, L.-E.; Zámocký, M.; Margis-Pinheiro, M. Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida. Antioxidants 2021, 10, 597. https://doi.org/10.3390/antiox10040597

AMA Style

Lazzarotto F, Menguer PK, Del-Bem L-E, Zámocký M, Margis-Pinheiro M. Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida. Antioxidants. 2021; 10(4):597. https://doi.org/10.3390/antiox10040597

Chicago/Turabian Style

Lazzarotto, Fernanda, Paloma K. Menguer, Luiz-Eduardo Del-Bem, Marcel Zámocký, and Márcia Margis-Pinheiro. 2021. "Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida" Antioxidants 10, no. 4: 597. https://doi.org/10.3390/antiox10040597

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