animal Peroxidase
3641842
Revisiting the Non Animal Peroxidase Superfamily.
Peroxidases reduce peroxide through substrate oxidation in order to alleviate oxidative stress in aerobic organisms. Since the initial description of the non animal peroxidase superfamily, great effort has been made to characterize this large and heterogeneous group of proteins. Next generation sequencing data have permitted an in depth study of the molecular evolution of this superfamily and allowed us to perform a phylogenetic reconstruction. Through this analysis, we identified two additional class I members and, here, we discuss the similarities and differences among members of this class. Our results provide new insights into the organization of these antioxidant enzymes, allowing us to propose a new model for the emergence and evolution of this superfamily.
Trends in plant science
Fernanda Lazzarotto Andreia Carina Turchetto-Zolet Marcia Margis-Pinheiro
18752741
Identification of a Novel Calcium Binding Motif Based on the Detection of Sequence Insertions in the Animal Peroxidase Domain of Bacterial Proteins
Proteins of the animal heme peroxidase (ANP) superfamily differ greatly in size since they have either one or two catalytic domains that match profile PS50292. The orf PP_2561 of Pseudomonas putida KT2440 that we have called PepA encodes a two domain ANP. The alignment of these domains with those of PepA homologues revealed a variable number of insertions with the consensus G x D G x x [GN] [TN] x D D. This motif has also been detected in the structure of pseudopilin (pdb 3G20) where it was found to be involved in Ca2+ coordination although a sequence analysis did not reveal the presence of any known calcium binding motifs in this protein. Isothermal titration calorimetry revealed that a peptide containing this consensus motif bound specifically calcium ions with affinities ranging between 33 79 uM depending on the pH. Microcalorimetric titrations of the purified N terminal ANP like domain of PepA revealed Ca2+ binding with a KD of 12 uM and stoichiometry of 1.25 calcium ions per protein monomer. This domain exhibited peroxidase activity after its reconstitution with heme. These data led to the definition of a novel calcium binding motif that we have termed PERCAL and which was abundantly present in animal peroxidase like domains of bacterial proteins. Bacterial heme peroxidases thus possess two different types of calcium binding motifs, namely PERCAL and the related hemolysin type calcium binding motif, with the latter being located outside the catalytic domains and in their C terminal end. A phylogenetic tree of ANP like catalytic domains of bacterial proteins with PERCAL motifs, including single domain peroxidases, was divided into two major clusters, representing domains with and without PERCAL motif containing insertions. We have verified that the recently reported classification of bacterial heme peroxidases in two families (cd09819 and cd09821) is unrelated to these insertions. Sequences matching PERCAL were detected in all kingdoms of life.
PloS one
Saray Santamaria-Hernando Tino Krell Maria Isabel Ramos-Gonzalez
4568868
Prokaryotic origins of the non animal peroxidase superfamily and organelle mediated transmission to eukaryotes.
Members of the superfamily of plant, fungal, and bacterial peroxidases are known to be present in a wide variety of living organisms. Extensive searching within sequencing projects identified organisms containing sequences of this superfamily. Class I peroxidases, cytochrome c peroxidase (CcP) ascorbate peroxidase (APx) and catalase peroxidase (CP) are known to be present in bacteria, fungi, and plants, but have now been found in various protists. CcP sequences were detected in most mitochondria possessing organisms except for green plants, which possess only ascorbate peroxidases. APx sequences had previously been observed only in green plants but were also found in chloroplastic protists, which acquired chloroplasts by secondary endosymbiosis. CP sequences that are known to be present in prokaryotes and in Ascomycetes were also detected in some Basidiomycetes and occasionally in some protists. Class II peroxidases are involved in lignin biodegradation and are found only in the Homobasidiomycetes. In fact class II peroxidases were identified in only three orders, although degenerate forms were found in different Pezizomycota orders. Class III peroxidases are specific for higher plants, and their evolution is thought to be related to the emergence of the land plants. We have found, however, that class III peroxidases are present in some green algae, which predate land colonization. The presence of peroxidases in all major phyla (except vertebrates) makes them powerful marker genes for understanding the early evolutionary events that led to the appearance of the ancestors of each eukaryotic group.
Genomics
Filippo Passardi Nenad Bakalovic Felipe Karam Teixeira Marcia Margis-Pinheiro Claude Penel Christophe Dunand
81741913
Structure Function Relationships Amongst Members of the Animal Peroxidase Family of Proteins
Heme peroxidases contain the well known heme b as prosthetic group and use hydrogen peroxide as electron acceptor to catalyze the oxidation of a large number of substrates [1] On the basis of sequence homology they can be categorized into two super families (I and II) and are present in (I) bacteria, fungi, plants, and (II) animals [2, 3] The superfamily of animal peroxidases includes myeloperoxidase (MPO) eosinophil peroxidase (EPO) lactoperoxidase (LPO) thyroid peroxidase (TPO) and prostaglandin endoperoxide synthase (PGHS) These proteins are related members of the same gene superfamily (Table 15.1) The phylogenetic tree of these related members of animal peroxidases, as derived from ProtoMap [4] on the basis of known sequences, predicts some distinguishing divergences among members of the superfamily (Table 15.2)
Rosa Pia Ferrari Silvio Traversa
212751835
Global analysis of non animal peroxidases provides insights into the evolution of this gene family in the green lineage.
The non animal peroxidases belong to a superfamily of oxidoreductases that reduce the hydrogen peroxide and oxidize numerous substrates. Since their initial characterization in 1992, several advances have provided an understanding into the origin and evolution of this protein family. Here, we report the most comprehensive evolutionary analysis of non animal peroxidases using integrated in silico and biochemical approaches. Thanks to the availability of numerous genomic sequences from more than 2500 species belonging to 14 kingdoms together with expert and comprehensive annotation of peroxidase sequences centralized in a dedicated database, we have deepened our understanding of the evolutionary process underlying non animal peroxidases diversification through phylogenetic reconstructions. We analysed the distribution of all non animal peroxidases in more than 200 eukaryotic organisms in silico. First, we show that the presence or absence of non animal peroxidases correlate with the presence or absence of certain organelles or with specific biological processes. Scrutinizing in near 2000 organisms, we confirmed that ascorbate peroxidases (APx) and cytochromes c peroxidases (CcP) were detected respectively in chloroplast and mitochondria containing organisms. Plants, which contain both organelles, are an exception and contain only APxs without CcP. Class II peroxidases (CII Prx) only found in fungi with wood decay abilities and plant degradation and Class III peroxidases (CIII Prx) only detected in both streptophyte algae and land plants, have been subjected to large family expansion in the latter group. Moreover, we demonstrate that biochemical activities (APx, CcP and CIII Prx) assayed with protein extracts from 30 different eukaryotic organisms support the distribution of the sequences resulting from our in silico analysis. The biochemical results confirmed both the presence and classification of non animal peroxidase encoding sequences.
Journal of experimental botany
Duchesse Lacour Mbadinga Mbadinga Qiang Li Philippe Ranocha Yves Martinez Christophe Dunand
212836402
Global analysis of non animal peroxidases provides insights into the evolutionary basis of this gene family in green lineage
The non animal peroxidases belong to a superfamily of oxidoreductases that reduce the hydrogen peroxide and oxidize numerous substrates. Since their initial characterization in 1992, several advances have provided an understanding into the origin and evolutionary history of this family of proteins. Here, we report for the first time an exhaustive evolutionary analysis of non animal peroxidases using integrated in silico and biochemical strategies. Thanks to the availability of numerous genomic sequences from many species belonging to different kingdoms together with expert and exhaustive annotation of peroxidase sequences centralized in a dedicated database, we have deepened our understanding of the evolutionary process underlying non animal peroxidases through phylogenetic reconstructions. We analysed the distribution of all non animal peroxidases in more than 200 eukaryotic organisms in silico. First, we show that the presence or absence of non animal peroxidases can be correlated with the presence or absence of certain organelles or with specific biological processes. Examining a wide range of organisms, we confirmed that ascorbate peroxidases (APx) and cytochromes c peroxidases (CcP) were detected respectively in chloroplast and mitochondria containing organisms. Plants, which contain both organelles, are an exception and contain only APxs without CcP. Class III peroxidases (CIII Prx) were only detected in plants and Class II peroxidases (CII Prx) in fungi related to wood decay and plant degradation. Moreover, we demonstrate that biochemical activities (APx, CcP and CIII Prx) assayed in protein extracts obtained from 30 different eukaryotic organisms strongly support the distribution of the sequences resulting from our in silico analysis. The biochemical results confirmed both the presence and classification of non animal peroxidase encoding sequences.
Duchesse Lacour Mbadinga Mbadinga Qiang Li Philippe Ranocha Yves Martinez Endymion D Cooper Christophe Dunand
45965110
Identification and characterization of VPO1, a new animal heme containing peroxidase.
Animal heme containing peroxidases play roles in innate immunity, hormone biosynthesis, and the pathogenesis of inflammatory diseases. Using the peroxidase like domain of Duox1 as a query, we carried out homology searching of the National Center for Biotechnology Information database. Two novel heme containing peroxidases were identified in humans and mice. One, termed VPO1 for vascular peroxidase 1, exhibits its highest tissue expression in heart and vascular wall. A second, VPO2, present in humans but not in mice, is 63% identical to VPO1 and is highly expressed in heart. The peroxidase homology region of VPO1 shows 42% identity to myeloperoxidase and 57% identity to the insect peroxidase peroxidasin. A molecular model of the VPO1 peroxidase region reveals a structure very similar to that of known peroxidases, including a conserved heme binding cavity, critical catalytic residues, and a calcium binding site. The absorbance spectra of VPO1 are similar to those of lactoperoxidase, and covalent attachment of the heme to VPO1 protein was demonstrated by chemiluminescent heme staining. VPO1 purified from heart or expressed in HEK cells is catalytically active, with a K(m) for H(2)O(2) of 1.5 mM. When co expressed in cells, VPO1 can use H(2)O(2) produced by NADPH oxidase enzymes. VPO1 is likely to carry out peroxidative reactions previously attributed exclusively to myeloperoxidase in the vascular system.
Free radical biology medicine
Guangjie Cheng John C Salerno Zehong Cao Patrick J Pagano John David Lambeth
9290090
Reversible near infrared fluorescent probe introducing tellurium to mimetic glutathione peroxidase for monitoring the redox cycles between peroxynitrite and glutathione in vivo.
The redox homeostasis between peroxynitrite and glutathione is closely associated with the physiological and pathological processes, e.g. vascular tissue prolonged relaxation and smooth muscle preparations, attenuation hepatic necrosis, and activation matrix metalloproteinase 2. We report a near infrared fluorescent probe based on heptamethine cyanine, which integrates with telluroenzyme mimics for monitoring the changes of ONOO( /GSH levels in cells and in vivo. The probe can reversibly respond to ONOO( and GSH and exhibits high selectivity, sensitivity, and mitochondrial target. It is successfully applied to visualize the changes of redox cycles during the outbreak of ONOO( and the antioxidant GSH repair in cells and animal. The probe would provide a significant advance on the redox events involved in the cellular redox regulation.
Journal of the American Chemical Society
Fabiao Yu Peng Li Bingshuai Wang Keli Han
16323689
Concentrations of haptoglobin in bovine plasma determined by ELISA or a colorimetric method based on peroxidase activity.
The objective was to compare different procedures for determination of haptoglobin in bovine plasma. Nine Angus steers were vaccinated against Mannheimia haemolytica to stimulate an acute phase response. Blood samples were collected immediately prior to vaccination (day 0) and on days 1, 3, 5, 7 and 10. Plasma samples were frozen in duplicates at 80 degC. One set of the duplicates was analysed for haptoglobin concentrations using a commercial ELISA kit. A day effect was detected (p 0.01) because haptoglobin peaked on day 3 and returned to baseline on day 7 relative to vaccination. The second duplicate was analysed using a procedure that measures haptoglobin haemoglobin complexing by estimating differences in peroxidase activity (CPPA) with results expressed as optical density. Further, based on the ELISA results, the plasma sample with the greatest haptoglobin concentration was also serially diluted into a plasma sample with negligible haptoglobin concentration from the same steer (1:1 through 1:1024 dilution) These dilutions were used within the CPPA method to generate a standard curve and estimate plasma haptoglobin concentrations (CPPA STD) A linear standard curve was generated (r(2) 0.99) A day effect similar to the ELISA method was detected for the CPPA and CPPA STD methods (p 0.01) Results obtained from CPPA and ELISA methods were positively correlated (r 0.97; p 0.01) The values generated by the CPPA STD procedure were similar (p 0.38) compared to the values generated by the ELISA method. In conclusion, assessing concentrations of haptoglobin in bovine plasma using the CPPA and CPPA STD methods generate highly correlated or similar results, respectively, compared to ELISA. Therefore, the CPPA STD and CPPA methods can be used as a less expensive alternative to ELISA to determine concentrations or monitor changes in plasma haptoglobin in bovine samples.
Journal of animal physiology and animal nutrition
Reinaldo Fernandes Cooke John D Arthington
29037363
Selenium Enriched Foods Are More Effective at Increasing Glutathione Peroxidase (GPx) Activity Compared with Selenomethionine: A Meta Analysis
Selenium may play a beneficial role in multi factorial illnesses with genetic and environmental linkages via epigenetic regulation in part via glutathione peroxidase (GPx) activity. A meta analysis was undertaken to quantify the effects of dietary selenium supplementation on the activity of overall GPx activity in different tissues and animal species and to compare the effectiveness of different forms of dietary selenium. GPx activity response was affected by both the dose and form of selenium (p 0.001) There were differences between tissues on the effects of selenium supplementation on GPx activity (p 0.001) however, there was no evidence in the data of differences between animal species (p 0.95) The interactions between dose and tissue, animal species and form were significant (p 0.001) Tissues particularly sensitive to changes in selenium supply include red blood cells, kidney and muscle. The meta analysis identified that for animal species selenium enriched foods were more effective than selenomethionine at increasing GPx activity.
Nutrients
Emma N Bermingham John E Hesketh Bruce R Sinclair John P Koolaard Nicole C Roy