Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida
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 famil...
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MDPI AG
2021-04-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/10/4/597 |
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| author | Fernanda Lazzarotto Paloma Koprovski Menguer Luiz-Eduardo Del-Bem Marcel Zámocký Márcia Margis-Pinheiro |
| author_facet | Fernanda Lazzarotto Paloma Koprovski Menguer Luiz-Eduardo Del-Bem Marcel Zámocký Márcia Margis-Pinheiro |
| author_sort | Fernanda Lazzarotto |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T12:22:35Z |
| format | Article |
| id | doaj.art-c90e85c49d9a429daae9f308841a8585 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T12:22:35Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-c90e85c49d9a429daae9f308841a85852023-11-21T15:23:24ZengMDPI AGAntioxidants2076-39212021-04-0110459710.3390/antiox10040597Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal ArchaeplastidaFernanda Lazzarotto0Paloma Koprovski Menguer1Luiz-Eduardo Del-Bem2Marcel Zámocký3Márcia Margis-Pinheiro4Centro de Biotecnologia, Programa de Pós-Graduação em Biologia Celular e Molecular, Universidade Federal do Rio Grande do Sul, Porto Alegre 91509-900, BrazilCentro de Biotecnologia, Programa de Pós-Graduação em Biologia Celular e Molecular, Universidade Federal do Rio Grande do Sul, Porto Alegre 91509-900, BrazilDepartamento de Botânica, Instituto de Ciências Biológicas, Universidade Federal De Minas Gerais, Belo Horizonte 31270-901, BrazilLaboratory of Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, SK-84551 Bratislava, SlovakiaCentro de Biotecnologia, Programa de Pós-Graduação em Biologia Celular e Molecular, Universidade Federal do Rio Grande do Sul, Porto Alegre 91509-900, BrazilAscorbate 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.https://www.mdpi.com/2076-3921/10/4/597ascorbate peroxidase—APXAPX-RAPX-Lcatalytic sitessubstrateprotein divergence |
| spellingShingle | Fernanda Lazzarotto Paloma Koprovski Menguer Luiz-Eduardo Del-Bem Marcel Zámocký Márcia Margis-Pinheiro Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida Antioxidants ascorbate peroxidase—APX APX-R APX-L catalytic sites substrate protein divergence |
| title | Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida |
| title_full | Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida |
| title_fullStr | Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida |
| title_full_unstemmed | Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida |
| title_short | Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida |
| title_sort | ascorbate peroxidase neofunctionalization at the origin of apx r and apx l evidence from basal archaeplastida |
| topic | ascorbate peroxidase—APX APX-R APX-L catalytic sites substrate protein divergence |
| url | https://www.mdpi.com/2076-3921/10/4/597 |
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