Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium

Gold, Michael H.; Kuwahara, Masaaki; Chiu, A A; Glenn, Jeffrey K.

doi:10.1016/0003-9861(84)90280-7

Cited by 320 publications

(133 citation statements)

References 26 publications

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“…Repeated and systematic attempts have failed to identify LiP (or VP) activity in C. subvermispora cultures, but substantial evidence implicates MnP in ligninolysis (e.g., refs 7, 8). First discovered in P. chrysosporium cultures, this enzyme oxidizes Mn 2+ to Mn 3+ , using H 2 O 2 as an oxidant (9,10). MnP cannot directly cleave the dominant nonphenolic structures within lignin, but it has been suggested that oxidation may be mediated by lipid peroxidation mechanisms that are promoted by Mn 3+ (3).…”

Section: Environmental Sciences Sustainability Sciencementioning

confidence: 99%

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

Fernández‐Fueyo

Ruíz-Dueñas

Ferreira

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

270

235

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Efficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium . Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium , respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli , the enzymes were shown to oxidize high redox potential substrates, but not Mn 2+ . Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium .

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Section: Environmental Sciences Sustainability Sciencementioning

confidence: 99%

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

Fernández‐Fueyo

Ruíz-Dueñas

Ferreira

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

270

235

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“…chrysosporium as previously described [1,3], and dialyzed against deionized water. The H202 concentration was determined as described [10].…”

Section: Methodsmentioning

confidence: 99%

“…Phanerochaete chrysosporium [1][2][3]. The H202-oxidized states of LiP [4][5][6] are similar to those of HRP [7].…”

Section: Introductionmentioning

confidence: 99%

“…The H202-oxidized states of LiP [4][5][6] are similar to those of HRP [7]. The enzyme has an unusually low pH optimum (<3.0) [5,6] and catalyzes the H202-dependent oxidation of a variety of lignin model compounds [1][2][3]8,9]. At pH 3.0 in the presence of 20 equivalents of H202 and in the absence of a reducing substrate, lignin peroxidase compound III (LiPIII) is formed readily [6].…”

Section: Introductionmentioning

confidence: 99%

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Lignin peroxidase compound III

Wariishi¹,

Gold²

1989

FEBS Letters

Self Cite

104

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At pH 3.0 in the absence of a reducing substrate and the presence of only 20 equivalents of I-I~O z, lignin peroxidase (LIP) is readily converted to LiP compound III (LiPIII) (Fe(IIl)O~-complex). LiPIII which is produced via the reaction of LiP compound II (LiPII) with H202 is not part of the peroxidase catalytic cycle, and is readily and irreversibly inactivated. Veratryl alcohol (VA), a Phanerochaete chrysosporium secondary metabolite, protects the enzyme from inactivation via two mechanisms. Acting as a substrate, VA reduces LiPII to regenerate the native enzyme. Secondly, the binding of VA to LiPIII rapidly displaces O~-/HO~, thereby converting LiPIII directly to the native enzyme. VA is not consumed during this displacement reaction. These results help to explain the role of VA in stabilizing the enzyme in the presence of excess HzO 2.

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“…Using this strategy, yeast cytochrome c peroxidase (2) and chloroplast ascorbate peroxidase (3) were classified as class I peroxidases on account of their prokaryotic source. Representatives of class II include lignin peroxidase (LiP) 2 (4), manganese peroxidase (MnP) (5), and versatile peroxidase (6,7), whereas class III contains horseradish peroxidase (HRP) (8) and barley grain peroxidase (BGP) (9). This classification has been widely applied to most known peroxidases, with the exception of chloroperoxidase (CPO) isolated from the fungus, Caldariomyces fumago, which lacks primary structural homology with other peroxidases (10,11).…”

mentioning

confidence: 99%

DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

Sugano

Muramatsu

Ichiyanagi

et al. 2007

Journal of Biological Chemistry

207

285

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DyP, a unique dye-decolorizing enzyme from the fungus Thanatephorus cucumeris Dec 1, has been classified as a peroxidase but lacks homology to almost all other known plant peroxidases. The primary structure of DyP shows moderate sequence homology to only two known proteins: the peroxidedependent phenol oxidase, TAP, and the hypothetical peroxidase, cpop21. Here, we show the first crystal structure of DyP and reveal that this protein has a unique tertiary structure with a distal heme region that differs from that of most other peroxidases. DyP lacks an important histidine residue known to assist in the formation of a Fe 4؉ oxoferryl center and a porphyrinbased cation radical intermediate (compound I) during the action of ubiquitous peroxidases. Instead, our tertiary structural and spectrophotometric analyses of DyP suggest that an aspartic acid and an arginine are involved in the formation of compound I. Sequence analysis reveals that the important aspartic acid and arginine mentioned above and histidine of the heme ligand are conserved among DyP, TAP, and cpop21, and structural and phylogenetic analyses confirmed that these three enzymes do not belong to any other families of peroxidase. These findings, which strongly suggest that DyP is a representative heme peroxidase from a novel family, should facilitate the identification of additional new family members and accelerate the classification of this novel peroxidase family.Peroxidases have been systematically researched for more than 70 years. Fifteen years ago, Welinder (1) proposed the concept of a "plant peroxidase superfamily" comprising classes I, II, and III, based on primary sequence alignments and isolation from prokaryotes, fungi, and plants, respectively. Using this strategy, yeast cytochrome c peroxidase (2) and chloroplast ascorbate peroxidase (3) were classified as class I peroxidases on account of their prokaryotic source. Representatives of class II include lignin peroxidase (LiP) 2 (4), manganese peroxidase (MnP) (5), and versatile peroxidase (6, 7), whereas class III contains horseradish peroxidase (HRP) (8) and barley grain peroxidase (BGP) (9). This classification has been widely applied to most known peroxidases, with the exception of chloroperoxidase (CPO) isolated from the fungus, Caldariomyces fumago, which lacks primary structural homology with other peroxidases (10, 11). However, in contrast to the plant peroxidases, those from animals, including mammals, are yet to be categorized. To date, most of these enzymes have been grouped into the plant or animal peroxidase superfamily (12).So far, we isolated and characterized a novel extracellular peroxidase, DyP, from the fungus Thanatephorus cucumeris Dec 1 (13-16). DyP, a glycoprotein having one heme as a cofactor, has a molecular mass of 58 kDa and requires H 2 O 2 for all enzyme reactions, indicating that it functions as a peroxidase. DyP has several characteristics that distinguish it from all other peroxidases, including a particularly wide substrate specificity, a lack of homology to m...

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Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium

Cited by 320 publications

References 26 publications

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysis

Lignin peroxidase compound III

DyP, a Unique Dye-decolorizing Peroxidase, Represents a Novel Heme Peroxidase Family

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