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Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.

Zámocký M, Gasselhuber B, Furtmüller PG, Obinger C - Cell. Mol. Life Sci. (2014)

Bottom Line: In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain.Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily.We present and discuss their phylogeny, sequence signatures and putative biological function.

View Article: PubMed Central - PubMed

Affiliation: Division of Biochemistry, Department of Chemistry, VIBT, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria, marcel.zamocky@boku.ac.at.

ABSTRACT
Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function.

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Details of the phylogenetic tree (Fig. 1) focusing on the hybrid-type A peroxidase clades. Obtained bootstrap values are presented for the ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Subcellular location of hybrid A peroxidases is indicated
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Fig4: Details of the phylogenetic tree (Fig. 1) focusing on the hybrid-type A peroxidase clades. Obtained bootstrap values are presented for the ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Subcellular location of hybrid A peroxidases is indicated

Mentions: The investigation of hybrid-type A peroxidases (abbreviated as APx-CcP in PeroxiBase) started recently since it was found that they represent the missing link between ascorbate and cytochrome c peroxidases (Fig. 1). The presented detailed phylogenetic reconstruction (Fig. 4) additionally underlines that hybrid-type A peroxidases are also among first descendants of bifunctional catalase–peroxidases. Upon losing the (KatG-typical) C-terminal domain as well as the ability to dismutate hydrogen peroxide they became monofunctional peroxidases. It has been demonstrated frequently that ancient enzymes were promiscuous and thus multifunctional before evolving more specialized catalytic functions later during evolution [32].Fig. 4


Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.

Zámocký M, Gasselhuber B, Furtmüller PG, Obinger C - Cell. Mol. Life Sci. (2014)

Details of the phylogenetic tree (Fig. 1) focusing on the hybrid-type A peroxidase clades. Obtained bootstrap values are presented for the ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Subcellular location of hybrid A peroxidases is indicated
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4232752&req=5

Fig4: Details of the phylogenetic tree (Fig. 1) focusing on the hybrid-type A peroxidase clades. Obtained bootstrap values are presented for the ML method. Abbreviations of peroxidase names and corresponding ID numbers are taken from PeroxiBase. Subcellular location of hybrid A peroxidases is indicated
Mentions: The investigation of hybrid-type A peroxidases (abbreviated as APx-CcP in PeroxiBase) started recently since it was found that they represent the missing link between ascorbate and cytochrome c peroxidases (Fig. 1). The presented detailed phylogenetic reconstruction (Fig. 4) additionally underlines that hybrid-type A peroxidases are also among first descendants of bifunctional catalase–peroxidases. Upon losing the (KatG-typical) C-terminal domain as well as the ability to dismutate hydrogen peroxide they became monofunctional peroxidases. It has been demonstrated frequently that ancient enzymes were promiscuous and thus multifunctional before evolving more specialized catalytic functions later during evolution [32].Fig. 4

Bottom Line: In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain.Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily.We present and discuss their phylogeny, sequence signatures and putative biological function.

View Article: PubMed Central - PubMed

Affiliation: Division of Biochemistry, Department of Chemistry, VIBT, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria, marcel.zamocky@boku.ac.at.

ABSTRACT
Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function.

Show MeSH
Related in: MedlinePlus