Class III Peroxidases

Abstract Background Class III peroxidases (POD) proteins are widely present in the plant kingdom that are involved in a broad range of physiological processes including stress responses and lignin polymerization throughout the plant life cycle. At present, POD genes have been studied in Arabidopsis, rice, poplar, maize and Chinese pear, but there are no reports on the identification and function of POD gene family in Betula pendula. Results We identified 90 nonredundant POD genes in Betula pendula. (designated BpPODs). According to phylogenetic relationships, these POD genes were classified into 12 groups. The BpPODs are distributed in different numbers on the 14 chromosomes, and some BpPODs were located sequentially in tandem on chromosomes. In addition, we analyzed the conserved domains of BpPOD proteins and found that they contain highly conserved motifs. We also investigated their expression patterns in different tissues, the results showed that some BpPODs might play an important role in xylem, leaf, root and flower. Furthermore, under low temperature conditions, some BpPODs showed different expression patterns at different times. Conclusions The research on the structure and function of the POD genes in Betula pendula plays a very important role in understanding the growth and development process and the molecular mechanism of stress resistance. These results lay the theoretical foundation for the genetic improvement of Betula pendula.

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Biochemical and molecular evidence for the role of class III peroxidases in the resistance of carnation (Dianthus caryophyllus L) to Fusarium oxysporum f. sp. dianthi

Physiological and Molecular Plant Pathology ◽

10.1016/j.pmpp.2014.01.003 ◽

2014 ◽

Vol 85 ◽

pp. 42-52 ◽

Cited By ~ 4

Author(s):

Harold Duban Ardila ◽

Angelica María Torres ◽

Sixta Tulia Martínez ◽

Blanca Ligia Higuera

Keyword(s):

Fusarium Oxysporum ◽

Dianthus Caryophyllus ◽

Molecular Evidence ◽

Class Iii ◽

Class Iii Peroxidases

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Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Journal of Biological Chemistry ◽

10.1074/jbc.m402384200 ◽

2004 ◽

Vol 279 (37) ◽

pp. 39000-39009 ◽

Cited By ~ 37

Author(s):

Roberta Pierattelli ◽

Lucia Banci ◽

Nigel A. J. Eady ◽

Jacques Bodiguel ◽

Jamie N. Jones ◽

...

Keyword(s):

Class I ◽

Class Iii ◽

Class Iii Peroxidases

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Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions

International Journal of Molecular Sciences ◽

10.3390/ijms19102876 ◽

2018 ◽

Vol 19 (10) ◽

pp. 2876 ◽

Cited By ~ 9

Author(s):

Sabine Lüthje ◽

Teresa Martinez-Cortes

Keyword(s):

Plasma Membranes ◽

Secretory Pathway ◽

In Silico Analysis ◽

Class Iii ◽

Membrane Repair ◽

Protein Protein Interaction ◽

Thale Cress ◽

Membrane Bound ◽

Class Iii Peroxidases ◽

Detergent Resistant Membrane

Class III peroxidases are heme-containing proteins of the secretory pathway with a high redundance and versatile functions. Many soluble peroxidases have been characterized in great detail, whereas only a few studies exist on membrane-bound isoenzymes. Membrane localization of class III peroxidases has been demonstrated for tonoplast, plasma membrane and detergent resistant membrane fractions of different plant species. In silico analysis revealed transmembrane domains for about half of the class III peroxidases that are encoded by the maize (Zea mays) genome. Similar results have been found for other species like thale-cress (Arabidopsis thaliana), barrel medic (Medicago truncatula) and rice (Oryza sativa). Besides this, soluble peroxidases interact with tonoplast and plasma membranes by protein–protein interaction. The topology, spatiotemporal organization, molecular and biological functions of membrane-bound class III peroxidases are discussed. Besides a function in membrane protection and/or membrane repair, additional functions have been supported by experimental data and phylogenetics.

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Analysis of Arabidopsis thaliana Redox Gene Network Indicates Evolutionary Expansion of Class III Peroxidase in Plants

Scientific Reports ◽

10.1038/s41598-019-52299-y ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 5

Author(s):

Raffael Azevedo de Carvalho Oliveira ◽

Abraão Silveira de Andrade ◽

Danilo Oliveira Imparato ◽

Juliana Gabriela Silva de Lima ◽

Ricardo Victor Machado de Almeida ◽

...

Keyword(s):

Gene Network ◽

Redox System ◽

Plant Evolution ◽

Evolutionary Origin ◽

Class Iii ◽

Ros Metabolism ◽

History Of ◽

Thiol Redox ◽

Public Repositories ◽

Class Iii Peroxidases

Abstract Reactive oxygen species (ROS) are byproducts of aerobic metabolism and may cause oxidative damage to biomolecules. Plants have a complex redox system, involving enzymatic and non-enzymatic compounds. The evolutionary origin of enzymatic antioxidant defense in plants is yet unclear. Here, we describe the redox gene network for A. thaliana and investigate the evolutionary origin of this network. We gathered from public repositories 246 A. thaliana genes directly involved with ROS metabolism and proposed an A. thaliana redox gene network. Using orthology information of 238 Eukaryotes from STRINGdb, we inferred the evolutionary root of each gene to reconstruct the evolutionary history of A. thaliana antioxidant gene network. We found two interconnected clusters: one formed by SOD-related, Thiol-redox, peroxidases, and other oxido-reductase; and the other formed entirely by class III peroxidases. Each cluster emerged in different periods of evolution: the cluster formed by SOD-related, Thiol-redox, peroxidases, and other oxido-reductase emerged before opisthokonta-plant divergence; the cluster composed by class III peroxidases emerged after opisthokonta-plant divergence and therefore contained the most recent network components. According to our results, class III peroxidases are in expansion throughout plant evolution, with new orthologs emerging in each evaluated plant clade divergence.

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Phylogeny, topology, structure and functions of membrane-bound class III peroxidases in vascular plants

Phytochemistry ◽

10.1016/j.phytochem.2010.11.023 ◽

2011 ◽

Vol 72 (10) ◽

pp. 1124-1135 ◽

Cited By ~ 22

Author(s):

Sabine Lüthje ◽

Claudia-Nicole Meisrimler ◽

David Hopff ◽

Benjamin Möller

Keyword(s):

Vascular Plants ◽

Class Iii ◽

Topology Structure ◽

Membrane Bound ◽

Class Iii Peroxidases ◽

Structure And Functions

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Suspension cell culture as a tool for the characterization of class III peroxidases in sugarcane

Plant Physiology and Biochemistry ◽

10.1016/j.plaphy.2012.10.015 ◽

2013 ◽

Vol 62 ◽

pp. 1-10 ◽

Cited By ~ 19

Author(s):

Igor Cesarino ◽

Pedro Araújo ◽

Adriana Franco Paes Leme ◽

Silvana Creste ◽

Paulo Mazzafera

Keyword(s):

Cell Culture ◽

Suspension Cell ◽

Suspension Cell Culture ◽

Class Iii ◽

Class Iii Peroxidases

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Preparation of aqueous polyaniline-vesicle suspensions with class III peroxidases. Comparison between horseradish peroxidase isoenzyme C and soybean peroxidase

Chemical Papers ◽

10.2478/s11696-013-0307-y ◽

2013 ◽

Vol 67 (8) ◽

Cited By ~ 21

Author(s):

Katja Junker ◽

Ivan Gitsov ◽

Nick Quade ◽

Peter Walde

Keyword(s):

Horseradish Peroxidase ◽

Enzyme Stability ◽

Class Iii ◽

Salt Form ◽

Reaction Conditions ◽

Soybean Peroxidase ◽

Peroxidase Isoenzyme ◽

Complete Inactivation ◽

Class Iii Peroxidases ◽

Optimal Reaction

AbstractAniline was polymerised enzymatically in aqueous solution at pH = 4.3 and 25°C in the presence of submicrometer-sized vesicles formed from sodium bis(2-ethylhexyl)sulphosuccinate (AOT). H2O2 served as oxidant and the enzyme used was either horseradish peroxidase isoenzyme C (HRPC) or soybean peroxidase (SBP), both being class III peroxidases. From previous studies with HRPC, it is known that stable vesicle suspensions containing the emeraldine salt form of polyaniline (PANI-ES) can be obtained within 1–2 days with a 90–95 % yield, provided that optimal reaction conditions are applied. Unfortunately, HRPC becomes inactivated during polymerisation. In the present study, a linear dendritic block copolymer was added to HRPC, resulting in higher operational enzyme stability; the stabilising effect, however, was too small to afford a substantial decrease in the required amount of enzyme. Moreover, replacing HRPC with SBP was of no advantage, although SBP is known to be more stable towards inactivation by H2O2 than HRPC. By contrast, SBP was found to be much slower in oxidising aniline, and complete inactivation of SBP occurred before all the aniline monomers were oxidised, leading to low yields and the formation of over-oxidised products. The same was observed for HRP isoenzyme A2. Reactions without vesicles indicated that peroxidase inactivation was probably caused by PANI-ES.

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