Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: Potential oxidation sites for oxidative polymerization of lignin

Sasaki, Susumu; Nonaka, Daisuke; Wariishi, Hiroyuki; Tsutsumi, Yuji; Kondo, Ryuichiro

doi:10.1016/j.phytochem.2007.08.020

Cited by 33 publications

(34 citation statements)

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“…Both peroxidases and laccases have been shown to be active in woodforming tissues of Populus and to be capable of polymerizing both monomethoxylated (guaiacyl G) and bimethoxylated (syringyl S) monolignols into lignin-like polymers in vitro (Christensen et al, 1998;Ranocha et al, 1999;Sasaki et al, 2004Sasaki et al, , 2008. More recently, laccases LAC4/IRX12, LAC11, and LAC17 (Zhao et al, 2013) were demonstrated to act redundantly during vessel element and fiber lignification.…”

Section: Spatially Separated Expression Of Phenoloxidases May Enable mentioning

confidence: 99%

AspWood: High-Spatial-Resolution Transcriptome Profiles Reveal Uncharacterized Modularity of Wood Formation in Populus tremula

et al. 2017

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Trees represent the largest terrestrial carbon sink and a renewable source of ligno-cellulose. There is significant scope for yield and quality improvement in these largely undomesticated species, and efforts to engineer elite varieties will benefit from improved understanding of the transcriptional network underlying cambial growth and wood formation. We generated highspatial-resolution RNA sequencing data spanning the secondary phloem, vascular cambium, and wood-forming tissues of Populus tremula. The transcriptome comprised 28,294 expressed, annotated genes, 78 novel protein-coding genes, and 567 putative long intergenic noncoding RNAs. Most paralogs originating from the Salicaceae whole-genome duplication had diverged expression, with the exception of those highly expressed during secondary cell wall deposition. Coexpression network analyses revealed that regulation of the transcriptome underlying cambial growth and wood formation comprises numerous modules forming a continuum of active processes across the tissues. A comparative analysis revealed that a majority of these modules are conserved in Picea abies. The high spatial resolution of our data enabled identification of novel roles for characterized genes involved in xylan and cellulose biosynthesis, regulators of xylem vessel and fiber differentiation and lignification. An associated web resource (AspWood, http://aspwood.popgenie.org) provides interactive tools for exploring the expression profiles and coexpression network.

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Section: Spatially Separated Expression Of Phenoloxidases May Enable mentioning

confidence: 99%

AspWood: High-Spatial-Resolution Transcriptome Profiles Reveal Uncharacterized Modularity of Wood Formation in Populus tremula

et al. 2017

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“…The class III plant POXs often contain several tyrosines [95], probably acting as protein anchoring positions for covalent linkages to the plant cell walls [96] Regarding their catalytic functions and protein sequence phylogeny, both AcLnP and TcPOX resemble CIP and even the class III POXs more than LIP, MNPs or VP, and therefore are not classified into the LMPs.…”

Section: Structural and Phylogenetic Features Of The Lmpsmentioning

confidence: 99%

Lignin‐modifying enzymes in filamentous basidiomycetes – ecological, functional and phylogenetic review

Lundell

Mäkelä

Hildén

2010

J. Basic Microbiol.

398

236

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Filamentous fungi owe powerful abilities for decomposition of the extensive plant material, lignocellulose, and thereby are indispensable for the Earth's carbon cycle, generation of soil humic matter and formation of soil fine structure. The filamentous wood-decaying fungi belong to the phyla Basidiomycota and Ascomycota, and are unique organisms specified to degradation of the xylem cell wall components (cellulose, hemicelluloses, lignins and extractives). The basidiomycetous wood-decaying fungi form brackets, caps or resupinaceous (corticioid) fruiting bodies when growing on wood for dissemination of their sexual basidiospores. In particular, the ability to decompose the aromatic lignin polymers in wood is mostly restricted to the white rot basidiomycetes. The white-rot decay of wood is possible due to secretion of organic acids, secondary metabolites, and oxidoreductive metalloenzymes, heme peroxidases and laccases, encoded by divergent gene families in these fungi. The brown rot basidiomycetes obviously depend more on a non-enzymatic strategy for decomposition of wood cellulose and modification of lignin. This review gives a current ecological, genomic, and protein functional and phylogenetic perspective of the wood and lignocellulose-decaying basidiomycetous fungi.

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“…A single exception exists, among the more than 50 ligninolytic basidiomycete peroxidases cloned up to date, corresponding to a Trametes cervina LiP that includes in its structure a catalytic tyrosine involved in aromatic substrate oxidation (located at a different position than LiP Trp-171 and VP Trp-164) (28). However, formation of tyrosyl radicals has been suggested in other heme and nonheme proteins (29,30) including a plant peroxidase oxidizing bulky lignin precursor by a LRET mechanism (31).…”

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Protein Radicals in Fungal Versatile Peroxidase

Ruíz-Dueñas

Pogni

Morales

et al. 2009

Journal of Biological Chemistry

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Lignin-degrading peroxidases, a group of biotechnologically interesting enzymes, oxidize high redox potential aromatics via an exposed protein radical. Low temperature EPR of Pleurotus eryngii versatile peroxidase (VP) revealed, for the first time in a fungal peroxidase, the presence of a tryptophanyl radical in both the two-electron (VPI) and the one-electron (VPII) activated forms of the enzyme. Site-directed mutagenesis was used to substitute this tryptophan (Trp-164) by tyrosine and histidine residues. No changes in the crystal structure were observed, indicating that the modified behavior was due exclusively to the mutations introduced. EPR revealed the formation of tyrosyl radicals in both VPI and VPII of the W164Y variant. However, no protein radical was detected in the W164H variant, whose VPI spectrum indicated a porphyrin radical identical to that of the inactive W164S variant. Stopped-flow spectrophotometry showed that the W164Y mutation reduced 10-fold the apparent second-order rate constant for VPI reduction (k 2app ) by veratryl alcohol (VA), when compared with over 50-fold reduction in W164S, revealing some catalytic activity of the tyrosine radical. Its first-order rate constant (k 2 ) was more affected than the dissociation constant (K D2 ). Moreover, VPII reduction by VA was impaired by the above mutations, revealing that the Trp-164 radical was involved in catalysis by both VPI and VPII. The low first-order rate constant (k 3 ) values were similar for the W164Y, W164H, and W164S variants, indicating that the tyrosyl radical in VPII was not able to oxidize VA (in contrast with that observed for VPI). VPII self-reduction was also suppressed, revealing that Trp-164 is involved in this autocatalytic process.Lignin degradation, a key step for carbon recycling in land ecosystems and a central issue for industrial use of lignocellulosic biomass (e.g. in paper pulp manufacture and bioethanol production), is initiated in nature by 1-electron oxidation of the benzenic rings of lignin by specialized high redox potential fungal peroxidases (1-5). The latter include lignin peroxidase (LiP; 6 EC 1.11.1.14), first described in Phanerochaete chrysosporium together with manganese peroxidase (EC 1.11.1.13), and versatile peroxidase (VP; EC 1.11.1.16), described in Pleurotus and Bjerkandera species as a hybrid enzyme combining the catalytic properties of LiP and manganese peroxidase (6, 7). Oxidation of high redox potential aromatics, including nonphenolic lignin models, by LiP (8, 9) and VP (10) takes place at an exposed tryptophan by long range electron transfer (LRET) to heme in the 2-electron (Compound I) and 1-electron (Compound II) activated forms of the enzyme. This basically differs from Mn 2ϩ oxidation by manganese peroxidase (11) and VP (12) and oxidation of different phenolic substrates and dyes by classical plant peroxidases (13) that is produced by direct electron transfer to the activated heme cofactor.The existence of a tryptophan radical in a peroxidase (in this case neighbor to heme) has been re...

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Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: Potential oxidation sites for oxidative polymerization of lignin

Cited by 33 publications

References 35 publications

AspWood: High-Spatial-Resolution Transcriptome Profiles Reveal Uncharacterized Modularity of Wood Formation in Populus tremula

AspWood: High-Spatial-Resolution Transcriptome Profiles Reveal Uncharacterized Modularity of Wood Formation in Populus tremula

Lignin‐modifying enzymes in filamentous basidiomycetes – ecological, functional and phylogenetic review

Protein Radicals in Fungal Versatile Peroxidase

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