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Christian Obinger - One of the best experts on this subject based on the ideXlab platform.
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Evolution of structure and function of human Peroxidases
Free Radical Biology and Medicine, 2018Co-Authors: Christian Obinger, Marcel Zámocký, Martina Paumann-page, Andrea Nicolussi, Paul G. FurtmüllerAbstract:Four heme superfamilies arose independently during evolution, which differ in overall fold, active site architecture and enzymatic activities. The redox cofactor is heme b or posttranslationally modified heme that is ligated by either histidine or cysteine. Here we describe the evolution of the Peroxidase-cyclooxygenase superfamily which is the only superfamily having the prosthetic group covalently linked via one-, two or three bonds with the protein. It is comprised of seven families with the chordata Peroxidases forming the latest evolutionary descendants including thyroid Peroxidase, lactoPeroxidase (LPO), eosinophil Peroxidase and myeloPeroxidase (MPO). Based on an updated phylogenetic tree, the available X-ray structures (MPO, LPO), biophysical and kinetic investigations, we analyse the evolution of structure and function of chordata heme Peroxidases as well as their relation to other (multidomain) families of this superfamily. Among other aspects the roles of the heme to protein linkages in redox chemistry and catalysis are presented. Finally, it is discussed how these biochemical properties are related to the physiological roles of these Peroxidases.
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fungal hybrid b heme Peroxidases unique fusions of a heme Peroxidase domain with a carbohydrate binding domain
Scientific Reports, 2017Co-Authors: Marcel Zámocký, Stefan Janecek, Christian ObingerAbstract:Heme Peroxidases, essential peroxide converting oxidoreductases are divided into four independently evolved superfamilies. Within the largest one – the Peroxidase-catalase superfamily - two hybrid lineages were described recently. Whereas Hybrid A heme Peroxidases represent intermediate enzymes between ascorbate Peroxidases and cytochrome c Peroxidases, Hybrid B heme Peroxidases are unique fusion proteins comprised of a conserved N-terminal heme Peroxidase domain and a C-terminal domain of various sugar binding motifs. So far these peculiar Peroxidases are only found in the kingdom of Fungi. Here we present a phylogenetic reconstruction of the whole superfamily with focus on Hybrid B Peroxidases. We analyse the domain assembly and putative structure and function of the newly discovered oligosaccharide binding domains. Two distinct carbohydrate binding modules (CBM21 and CBM34) are shown to occur in phytopathogenic ascomycetous orthologs of Hybrid B heme Peroxidases only. Based on multiple sequence alignment and homology modeling the structure-function relationships are discussed with respect to physiological function. A concerted action of peroxide cleavage with specific cell-wall carbohydrate binding can support phytopathogens survival within the plant host.
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Turning points in the evolution of Peroxidase–catalase superfamily: molecular phylogeny of hybrid heme Peroxidases
Cellular and Molecular Life Sciences, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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Turning points in the evolution of Peroxidase-catalase superfamily: molecular phylogeny of hybrid heme Peroxidases.
Cellular and molecular life sciences : CMLS, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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Molecular Phylogeny of Heme Peroxidases
Biocatalysis Based on Heme Peroxidases, 2010Co-Authors: Christian ObingerAbstract:All currently available gene sequences of heme Peroxidases can be phylogenetically divided in two superfamilies and three families. In this chapter, the phylogenetics and genomic distribution of each group are presented. Within the Peroxidase-cyclooxygenase superfamily, the main evolutionary direction devel- oped peroxidatic heme proteins involved in the innate immune defense system and in biosynthesis of (iodinated) hormones. The Peroxidase-catalase superfamily is widely spread mainly among bacteria, fungi, and plants, and particularly in Class I led to the evolution of bifunctional catalase-Peroxidases. Its numerous fungal representatives of Class II are involved in carbon recycling via lignin degradation, whereas Class III secretory Peroxidases from algae and plants are included in various forms of secondary metabolism. The family of di-heme Peroxidases are predominantly bacteria-inducible enzymes; however, a few corresponding genes were also detected in archaeal genomes. Four subfamilies of dyp-type Peroxidases capable of degradation of various xenobiotics are abundant mainly among bacteria
Marcel Zámocký - One of the best experts on this subject based on the ideXlab platform.
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Evolution of structure and function of human Peroxidases
Free Radical Biology and Medicine, 2018Co-Authors: Christian Obinger, Marcel Zámocký, Martina Paumann-page, Andrea Nicolussi, Paul G. FurtmüllerAbstract:Four heme superfamilies arose independently during evolution, which differ in overall fold, active site architecture and enzymatic activities. The redox cofactor is heme b or posttranslationally modified heme that is ligated by either histidine or cysteine. Here we describe the evolution of the Peroxidase-cyclooxygenase superfamily which is the only superfamily having the prosthetic group covalently linked via one-, two or three bonds with the protein. It is comprised of seven families with the chordata Peroxidases forming the latest evolutionary descendants including thyroid Peroxidase, lactoPeroxidase (LPO), eosinophil Peroxidase and myeloPeroxidase (MPO). Based on an updated phylogenetic tree, the available X-ray structures (MPO, LPO), biophysical and kinetic investigations, we analyse the evolution of structure and function of chordata heme Peroxidases as well as their relation to other (multidomain) families of this superfamily. Among other aspects the roles of the heme to protein linkages in redox chemistry and catalysis are presented. Finally, it is discussed how these biochemical properties are related to the physiological roles of these Peroxidases.
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fungal hybrid b heme Peroxidases unique fusions of a heme Peroxidase domain with a carbohydrate binding domain
Scientific Reports, 2017Co-Authors: Marcel Zámocký, Stefan Janecek, Christian ObingerAbstract:Heme Peroxidases, essential peroxide converting oxidoreductases are divided into four independently evolved superfamilies. Within the largest one – the Peroxidase-catalase superfamily - two hybrid lineages were described recently. Whereas Hybrid A heme Peroxidases represent intermediate enzymes between ascorbate Peroxidases and cytochrome c Peroxidases, Hybrid B heme Peroxidases are unique fusion proteins comprised of a conserved N-terminal heme Peroxidase domain and a C-terminal domain of various sugar binding motifs. So far these peculiar Peroxidases are only found in the kingdom of Fungi. Here we present a phylogenetic reconstruction of the whole superfamily with focus on Hybrid B Peroxidases. We analyse the domain assembly and putative structure and function of the newly discovered oligosaccharide binding domains. Two distinct carbohydrate binding modules (CBM21 and CBM34) are shown to occur in phytopathogenic ascomycetous orthologs of Hybrid B heme Peroxidases only. Based on multiple sequence alignment and homology modeling the structure-function relationships are discussed with respect to physiological function. A concerted action of peroxide cleavage with specific cell-wall carbohydrate binding can support phytopathogens survival within the plant host.
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Turning points in the evolution of Peroxidase–catalase superfamily: molecular phylogeny of hybrid heme Peroxidases
Cellular and Molecular Life Sciences, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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Turning points in the evolution of Peroxidase-catalase superfamily: molecular phylogeny of hybrid heme Peroxidases.
Cellular and molecular life sciences : CMLS, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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PeroxiBase: the Peroxidase database.
Phytochemistry, 2007Co-Authors: Filippo Passardi, Marcel Zámocký, Grégory Theiler, Claudia Cosio, Nicolas Rouhier, Felipe Teixera, Márcia Margis-pinheiro, Vassilios Ioannidis, Claude Penel, Laurent FalquetAbstract:Peroxidases (EC 1.11.1.x), which are encoded by small or large multigenic families, are involved in several important physiological and developmental processes. Analyzing their evolution and their distribution among various phyla could certainly help to elucidate the mystery of their extremely widespread and diversified presence in almost all living organisms. PeroxiBase was originally created for the exhaustive collection of class III Peroxidase sequences from plants (Bakalovic, N., Passardi, F., et al., 2006. PeroxiBase: a class III plant Peroxidase database. Phytochemistry 67, 534-539). The extension of the class III Peroxidase database to all proteins capable to reduce peroxide molecules appears as a necessity. Our database contains haem and non-haem Peroxidase sequences originated from annotated or not correctly annotated sequences deposited in the main repositories such as GenBank or UniProt KnowledgeBase. This new database will allow obtaining a global overview of the evolution the protein families and superfamilies capable of Peroxidase reaction. In this rapidly growing field, there is a need for continual updates and corrections of the Peroxidase protein sequences. Following the lack of unified nomenclature, we also introduced a unique abbreviation for each different family of Peroxidases. This paper thus aims to report the evolution of the PeroxiBase database, which is freely accessible through a web server (http://peroxibase.isb-sib.ch). In addition to new categories of Peroxidases, new specific tools have been created to facilitate query, classification and submission of Peroxidase sequences.
Martin Hofrichter - One of the best experts on this subject based on the ideXlab platform.
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Widespread Occurrence of Expressed Fungal Secretory Peroxidases in Forest Soils
2016Co-Authors: Harald Kellner, Donald R. Zak, Patricia Luis, Marek J. Pecyna, Florian Barbi, Danuta Kapturska, Martin HofrichterAbstract:Fungal secretory Peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell wall (lignin) and humus. They comprise three major groups: class II Peroxidases (including lignin Peroxidase, manganese Peroxidase, versatile Peroxidase and generic Peroxidase), dye-decolorizing Peroxidases, and heme-thiolate Peroxidases (e.g. unspecific/aromatic peroxygenase, chloroPeroxidase). Here, we have repeatedly observed a widespread expression of all major Peroxidase groups in leaf and needle litter across a range of forest ecosystems (e.g. Fagus, Picea, Acer, Quercus, and Populus spp.), which are widespread in Europe and North America. Manganese Peroxidases and unspecific peroxygenases were found expressed in all nine investigated forest sites, and dye-decolorizing Peroxidases were observed in five of the nine sites, thereby indicating biological significance of these enzymes for fungal physiology and ecosystem processes. Transcripts of selected secretory Peroxidase genes were also analyzed in pure cultures of several litter-decomposing species and other fungi. Using this information, we were able to match, in environmental litter samples, two manganese Peroxidase sequences to Mycena galopus and Mycena epipterygia and one unspecific peroxygenase transcript to Mycena galopus, suggesting an important role of this litter- and coarse woody debris-dwelling genus in the disintegratio
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Widespread Occurrence of Expressed Fungal Secretory Peroxidases in Forest Soils
PLoS ONE, 2014Co-Authors: Harald Kellner Mail, Patricia Luis, Marek J. Pecyna, Florian Barbi, Danuta Kapturska, Dirk Krüger, Donald R. Zak, Roland Marmeisse, Micheline Vandenbol, Martin HofrichterAbstract:Fungal secretory Peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell wall (lignin) and humus. They comprise three major groups: class II Peroxidases (including lignin Peroxidase, manganese Peroxidase, versatile Peroxidase and generic Peroxidase), dye-decolorizing Peroxidases, and heme-thiolate Peroxidases (e.g. unspecific/aromatic peroxygenase, chloroPeroxidase). Here, we have repeatedly observed a widespread expression of all major Peroxidase groups in leaf and needle litter across a range of forest ecosystems (e.g. Fagus, Picea, Acer, Quercus, and Populus spp.), which are widespread in Europe and North America. Manganese Peroxidases and unspecific peroxygenases were found expressed in all nine investigated forest sites, and dye-decolorizing Peroxidases were observed in five of the nine sites, thereby indicating biological significance of these enzymes for fungal physiology and ecosystem processes. Transcripts of selected secretory Peroxidase genes were also analyzed in pure cultures of several litter-decomposing species and other fungi. Using this information, we were able to match, in environmental litter samples, two manganese Peroxidase sequences to Mycena galopus and Mycena epipterygia and one unspecific peroxygenase transcript to Mycena galopus, suggesting an important role of this litter- and coarse woody debris-dwelling genus in the disintegration and transformation of litter aromatics and organic matter formation.
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Phenol oxidation by DyP-type Peroxidases in comparison to fungal and plant Peroxidases
Journal of Molecular Catalysis B: Enzymatic, 2014Co-Authors: Christiane Liers, Elizabet Aranda, Eric Strittmatter, Klaus Piontek, Dietmar A. Plattner, Holger Zorn, René Ullrich, Martin HofrichterAbstract:Abstract Over the last years, novel Peroxidases secreted by lignocellulose-degrading agaricomycetes have been discovered. Among them, the so-called DyP-type Peroxidases (DyPs) that are secreted under conditions close to nature (i.e. in wood cultures) are of particular interest, since they are able to oxidize diverse substrates including veratryl alcohol, non-phenolic lignin model dimers as well as recalcitrant phenols and dyes. In spite of their unique protein structure and their catalytic versatility, the estimation of the redox potential of this new Peroxidase group is still pending. To solve this problem, we used a catalytic approach developed by Ayala et al., 2007 [21] , which is based on the Marcus equation and the determination of the redox thermodynamics between heme-Peroxidase compound II and the resting state enzyme. Five fungal DyPs (among them four wild-type enzymes and one recombinant protein) were tested regarding phenol oxidation in comparison to other well-studied plant and fungal Peroxidases (soybean Peroxidase, SBP, Coprinopsis cinerea Peroxidase, CiP, lignin Peroxidase of Phanerochaete chrysosporium , LiP). DyP-type Peroxidases have a high affinity for phenols and can oxidize even recalcitrant representatives such as p -nitrophenol. Based on this “phenol oxidation method”, their redox potential was estimated to range between 1.10 ± 0.02 and 1.20 ± 0.1 V, which is between the values calculated for high-redox potential LiP (1.26 ± 0.17 V) and low-redox potential, phenol-oxidizing plant (0.93 ± 0.04 V for SBP) and fungal (1.06 ± 0.07 V for CiP) Peroxidases.
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dyp like Peroxidases of the jelly fungus auricularia auricula judae oxidize nonphenolic lignin model compounds and high redox potential dyes
Applied Microbiology and Biotechnology, 2010Co-Authors: Christiane Liers, Marek J. Pecyna, René Ullrich, Caroline Bobeth, Martin HofrichterAbstract:The jelly fungus Auricularia auricula-judae pro- duced an enzyme with manganese-independent Peroxidase activity during growth on beech wood (∼300 U l −1 ). The same enzymatic activity was detected and produced at larger scale in agitated cultures comprising of liquid, plant-based media (e.g. tomato juice suspensions) at levels up to 8,000 U l −1 . Two pure Peroxidase forms (A. auricula-judae Peroxidase (AjP I and AjP II) could be obtained from respective culture liquids by three chromatographic steps. Spectroscopic and electrophoretic analyses of the purified proteins revealed their heme and Peroxidase nature. The N-terminal amino acid sequence of AjP matched well with sequences of fungal enzymes known as "dye-decolorizing Peroxidases". Homology was found to the N-termini of Peroxidases from Marasmius scorodonius (up to 86%), Thanatephorus cucumeris (60%), and Termitomyces albuminosus (60%). Both enzyme forms catalyzed not only the conversion of typical Peroxidase substrates such as 2,6-dimethoxyphenol and 2,2'-azino-bis(3-ethylthiazoline-6- sulfonate) but also the decolorization of the high-redox potential dyes Reactive Blue 5 and Reactive Black 5, whereas manganese(II) ions (Mn 2+ ) were not oxidized. Most remarkable, however, is the finding that both AjPs oxidized nonphenolic lignin model compounds (veratryl alcohol; adlerol, a nonphenolic β-O-4 lignin model dimer) at low pH (maximum activity at pH 1.4), which indicates a certain ligninolytic activity of dye-decolorizing Peroxidases.
Paul G. Furtmüller - One of the best experts on this subject based on the ideXlab platform.
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Evolution of structure and function of human Peroxidases
Free Radical Biology and Medicine, 2018Co-Authors: Christian Obinger, Marcel Zámocký, Martina Paumann-page, Andrea Nicolussi, Paul G. FurtmüllerAbstract:Four heme superfamilies arose independently during evolution, which differ in overall fold, active site architecture and enzymatic activities. The redox cofactor is heme b or posttranslationally modified heme that is ligated by either histidine or cysteine. Here we describe the evolution of the Peroxidase-cyclooxygenase superfamily which is the only superfamily having the prosthetic group covalently linked via one-, two or three bonds with the protein. It is comprised of seven families with the chordata Peroxidases forming the latest evolutionary descendants including thyroid Peroxidase, lactoPeroxidase (LPO), eosinophil Peroxidase and myeloPeroxidase (MPO). Based on an updated phylogenetic tree, the available X-ray structures (MPO, LPO), biophysical and kinetic investigations, we analyse the evolution of structure and function of chordata heme Peroxidases as well as their relation to other (multidomain) families of this superfamily. Among other aspects the roles of the heme to protein linkages in redox chemistry and catalysis are presented. Finally, it is discussed how these biochemical properties are related to the physiological roles of these Peroxidases.
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Turning points in the evolution of Peroxidase–catalase superfamily: molecular phylogeny of hybrid heme Peroxidases
Cellular and Molecular Life Sciences, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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Turning points in the evolution of Peroxidase-catalase superfamily: molecular phylogeny of hybrid heme Peroxidases.
Cellular and molecular life sciences : CMLS, 2014Co-Authors: Marcel Zámocký, Bernhard Gasselhuber, Paul G. Furtmüller, Christian ObingerAbstract: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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The role of distal tryptophan in the bifunctional activity of catalase-Peroxidases.
Biochemical Society Transactions, 2001Co-Authors: Günther Regelsberger, Peter C. Loewen, Paul G. Furtmüller, Christa Jakopitsch, F. Rueker, J. Switala, Christian ObingerAbstract:Catalase-Peroxidases are bifunctional Peroxidases exhibiting an overwhelming catalase activity and a substantial Peroxidase activity. Here we present a kinetic study of the formation and reduction of the key intermediate compound I by probing the role of the conserved tryptophan at the distal haem cavity site. Two wild-type proteins and three mutants of Synechocystis catalase-Peroxidase (W122A and W122F) and Escherichia coli catalase-Peroxidase (W105F) have been investigated by steady-state and stopped-flow spectroscopy. W122F and W122A completely lost their catalase activity whereas in W105F the catalase activity was reduced by a factor of about 5000. However, the mutations did not influence both formation of compound I and its reduction by Peroxidase substrates. It was demonstrated unequivocally that the rate of compound I reduction by pyrogallol or o-dianisidine sometimes even exceeded that of the wild-type enzyme. This study demonstrates that the indole ring of distal Trp in catalase-Peroxidases is essential for the two-electron reduction of compound I by hydrogen peroxide but not for compound I formation or for Peroxidase reactivity (i.e. the one-electron reduction of compound I).
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Chapter 8:Mechanistic Aspects of Catalase-Peroxidase
Heme Peroxidases, 1Co-Authors: Bernhard Gasselhuber, Marcel Zámocký, Paul G. Furtmüller, Christa Jakopitsch, Christian ObingerAbstract:Catalase-Peroxidases (KatGs) belong to the Peroxidase-catalase superfamily and are found in bacteria, archaea, and lower eukaryotes including fungi. Despite having sequence and structural homology with monofunctional Peroxidases, KatGs are the only bifunctional Peroxidases with a dominating hydrogen peroxide dismutating activity which rivals that of typical catalases. Albeit both heme-containing catalases and KatGs catalyse the same reaction (2H2O2→2H2O+O2), the mechanism is clearly different. In KatG the activity is based on two redox cofactors, the iron-containing heme b and in close proximity the unique posttranslationally and endogenously generated Trp-Tyr-Met adduct. This strictly conserved adduct is essential for the pseudocatalytic activity of KatGs without influencing the Peroxidase activity. The key element in the proposed reaction mechanism is the formation of an adduct radical during turnover. This review accounts for the available literature for this mechanism and additionally discusses the role of the Peroxidase activity with a focus on the activation of the antitubercular pro-drug isoniazid by KatG.
D. L. Crawford - One of the best experts on this subject based on the ideXlab platform.
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Comparison of extracellular Peroxidase- and esterase-deficient mutants of Streptomyces viridosporus T7A.
Applied and environmental microbiology, 1992Co-Authors: T S Magnuson, D. L. CrawfordAbstract:Peroxidase-deficient mutants of the lignin-degrading bacterium Streptomyces viridosporus T7A were screened for their production of acid-precipitable polymeric lignin, extracellular Peroxidases and esterases, and immunoreactivities against a polyclonal antibody produced against electrophoretically purified Peroxidase isoform P3 of wild-type S. viridosporus. The mutants showed diminished abilities to solubilize lignin and produce acid-precipitable polymeric lignin. Their Peroxidase activities were decreased, and their esterase production patterns were altered. Western immunoblots demonstrated that the mutants produced proteins immunologically reactive with the antibody, but with different mobilities from those of wild-type proteins. These findings confirm a direct role for Peroxidases in lignin solubilization. They also indicate a possible role for esterases.
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Immunologic relatedness of extracellular ligninases from the actinomycetes Streptomyces viridosporus T7A and Streptomyces badius 252.
Applied biochemistry and biotechnology, 1991Co-Authors: T S Magnuson, D. L. Crawford, M A Roberts, G HertelAbstract:Four isoforms of the extracellular lignin Peroxidase of the ligninolytic actinomycete Streptomyces viridosporus T7A (ALip-P1, P2, P3, and P4) were individually purified by ultrafiltration and ammonium sulfate precipitation, followed by electro-elution using polyacrylamide gel electrophoresis. Three of the purified Peroxidases were compared for their immunologic relatedness by Western blot analysis using a polyclonal antibody preparation produced in rabbits against pure isoform P3. The anti-P3 antibody was also tested for its reactivity towards a lignin Peroxidase from the white-rot fungus Phanerochaete chrysosporium and another ligninolytic actinomycete Streptomyces badius 252. Results showed that Peroxidases ALip-P1 through ALip-P3 are immunologically related to one another. The Peroxidases of S. badius, but not the Peroxidase of P. chrysosporium, also reacted with the antibody, thus indicating that the lignin Peroxidases of S. viridosporus and S. badius are immunologically related. Based upon its specific affinity, lignin Peroxidase isoform ALip-P3 of S. viridosporus was readily purified using an anti-P3 antibody affinity column.
