DyP-type peroxidases: a promising and versatile class of enzymes

Colpa, Dana I.; Fraaije, Marco W.; Bloois, Edwin van

doi:10.1007/s10295-013-1371-6

Cited by 181 publications

(212 citation statements)

References 49 publications

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“…Additionally, DyP-type peroxidase also increased at 28°C in this species and subsequently decreased at 32°C in M. trossulus, possibly indicating a lower antioxidant capacity with exposure to this temperature. DyP-type peroxidases represent a novel family of heme-containing peroxidases whose function has yet to be determined (Colpa et al, 2014), although it is possible that they play a role in decreasing peroxynitrite (Trujillo et al, 2008). Thus, M. trossulus was unable to activate an antioxidant response at the highest temperature, a limitation likely contributing to its lower thermal tolerance.…”

Section: Temperature-induced Antioxidant Responsesmentioning

confidence: 99%

Proteomic responses to environmentally induced oxidative stress

Tomanek

2015

Journal of Experimental Biology

137

132

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Environmental (acute and chronic temperature, osmotic, hypoxic and pH) stress challenges the cellular redox balance and can lead to the increased production of reactive oxygen species (ROS). This review provides an overview of the reactions producing and scavenging ROS in the mitochondria, endoplasmic reticulum (ER) and peroxisome. It then compares these reactions with the findings of a number of studies investigating the proteomic responses of marine organisms to environmentally induced oxidative stress. These responses indicate that the thioredoxin-peroxiredoxin system is possibly more frequently recruited to scavenge H 2 O 2 than the glutathione system. Isoforms of superoxide dismutase (SOD) are not ubiquitously induced in parallel, suggesting that SOD scavenging activity is sometimes sufficient. The glutathione system plays an important role in some organisms and probably also contributes to protecting protein thiols during environmental stress. Synthesis pathways of cysteine and selenocysteine, building blocks for glutathione and glutathione peroxidase, also play an important role in scavenging ROS during stress. The increased abundance of glutaredoxin and DyP-type peroxidase suggests a need for regulating the deglutathionylation of proteins and scavenging of peroxynitrite. Reducing equivalents for these scavenging reactions are generated by proteins of the pentose phosphate pathway and by NADP-dependent isocitrate dehydrogenase. Furthermore, proteins representing reactions of the tricarboxylic acid cycle and the electron transport system generating NADH and ROS, including those of complex I, II and III, are frequently reduced in abundance with stress. Protein maturation in the ER likely represents another source of ROS during environmental stress, as indicated by simultaneous changes in ER chaperones and antioxidant proteins. Although there are still too few proteomic analyses of non-model organisms exposed to environmental stress for a general pattern to emerge, hyposaline and low pH stress show different responses from temperature and hypoxic stress. Furthermore, comparisons of closely related congeners differing in stress tolerance start to provide insights into biochemical processes contributing to adaptive differences, but more of these comparisons are needed to draw general conclusions. To fully take advantage of a systems approach, studies with longer time courses, including several tissues and more species comparisons are needed.

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Section: Temperature-induced Antioxidant Responsesmentioning

confidence: 99%

Proteomic responses to environmentally induced oxidative stress

Tomanek

2015

Journal of Experimental Biology

137

132

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“…Although the first DyP-type peroxidase was isolated from fungi, subsequent genome sequence analysis has revealed that this superfamily of enzymes is also prominent in bacteria. 13 DyP-type peroxidases typically require hydrogen peroxide to form the oxo-ferryl intermediates of the enzymes, which subsequently oxidize the mediator or the substrate.…”

Section: Cmentioning

confidence: 99%

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

et al. 2016

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Lignin is 1 of the 3 major components of lignocellulose. Its polymeric structure includes aromatic subunits that can be converted into high-value-added products, but this potential cannot yet been fully exploited because lignin is highly recalcitrant to degradation. Different approaches for the depolymerization of lignin have been tested, including pyrolysis, chemical oxidation, and hydrolysis under supercritical conditions. An additional strategy is the use of lignin-degrading enzymes, which imitates the natural degradation process. A versatile set of enzymes for lignin degradation has been identified, and research has focused on the production of recombinant enzymes in sufficient amounts to characterize their structure and reaction mechanisms. Enzymes have been analyzed individually and in combinations using artificial substrates, lignin model compounds, lignin and lignocellulose. Here we consider progress in the production of recombinant lignin-degrading peroxidases, the advantages and disadvantages of different expression hosts, and obstacles that must be overcome before such enzymes can be characterized and used for the industrial processing of lignin.

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“…In contrast to the other three classes of heme peroxidases described above, DyP-type peroxidases are not members of the classical plant/microbial peroxidase superfamily, due to differences in sequence, structure and function [66,67]. Therefore, they represent an additional superfamily of heme-containing peroxidases.…”

Section: +mentioning

confidence: 96%

Lignin Degradation Processes and the Purification of Valuable Products

Schoenherr¹,

Ebrahimi²,

Czermak³

2018

Lignin - Trends and Applications

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Lignin is a heterogeneous, phenolic and polydisperse biopolymer which resists degradation due to its aromatic and highly branched structure. Lignin is the most abundant renewable source of aromatic molecules on earth. The valorization of lignin could therefore provide a sustainable alternative to petroleum refineries for the production of valuable aromatic compounds. Even so, paper mills and lignocellulose feedstock biorefineries treat lignin largely as a waste product. In paper mills, 98% of technical lignin is incinerated for internal energy recovery while only 2% is used commercially (e.g. for the production of aromatics such as vanillin). The reasons for the underutilization of lignin include its recalcitrance to degradation and the challenge of separating mixtures of numerous degradation products. The successful valorization of lignin in the future thus depends on a broad understanding of biological and technical degradation processes, and the implementation of efficient product purification strategies. This article describes enzymatic, photocatalytic and thermochemical lignin degradation processes and considers purification methods for valuable lignin-derived degradation products. We focus on the potential of membrane-based separation technology, including data from our own recent research.

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DyP-type peroxidases: a promising and versatile class of enzymes

Cited by 181 publications

References 49 publications

Proteomic responses to environmentally induced oxidative stress

Proteomic responses to environmentally induced oxidative stress

Progress and obstacles in the production and application of recombinant lignin-degrading peroxidases

Lignin Degradation Processes and the Purification of Valuable Products

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