An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta

Muheim, Andreas; Waldner, Roland; Leisola, Matti; Fiechter, Armin

doi:10.1016/0141-0229(90)90039-s

Cited by 98 publications

(54 citation statements)

References 15 publications

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“…Subsequent studies focused on the Pleurotus eryngii enzyme, which was cloned and sequenced (Varela et al 1999), heterologously expressed (Varela et al 2001, Ruiz-Dueñas et al 2006, crystallized (Fernández et al 2009) and its reaction mechanisms investigated by a variety of techniques (Ferreira et al 2005(Ferreira et al , 2006(Ferreira et al , 2009(Ferreira et al , 2010(Ferreira et al , 2015Hernández-Ortega et al 2011a, b, 2012b. Then a Polyporales AAO was isolated from B. adusta (Muheim et al 1990). Although the above enzymes are known as secreted proteins (Hernández-Ortega et al 2012a), recognized signal peptides are missing from four of the 42 sequences from the 10 Polyporales genomes, including one sequence from B. adusta and two from D. squalens and P. chrysosporium.…”

Section: Discussionmentioning

confidence: 99%

“…(G. lucidum complex) and Phlebia brevispora-were sequenced (Hibbett et al 2013) and their different GMC gene families are analyzed here. Bjerkandera adusta is a strong lignin degrader, which produces AAO (Muheim et al 1990) together with ligninolytic peroxidases (Kimura et al 1991, Heinfling et al 1998. Some species of Ganoderma cause extensive wood delignification (González et al 1986;Martínez et al 1995Martínez et al , 2011 and little is known about GMC production by these fungi (Peláez et al 1995, Ralph et al 1996.…”

Section: Introductionmentioning

confidence: 99%

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A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Ferreira¹,

Carro²,

Serrano³

et al. 2015

Mycologia

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The genomes of three representative Polyporales (Bjerkandera adusta, Phlebia brevispora and a member of the Ganoderma lucidum complex) recently were sequenced to expand our knowledge on the diversity and distribution of genes involved in degradation of plant polymers in this Basidiomycota order, which includes most wood-rotting fungi. Oxidases, including members of the glucose-methanol-choline (GMC) oxidoreductase superfamily, play a central role in the above degradative process because they generate extracellular H 2 O 2 acting as the ultimate oxidizer in both white-rot and brown-rot decay. The survey was completed by analyzing the GMC genes in the available genomes of seven more species to cover the four Polyporales clades. First, an in silico search for sequences encoding members of the aryl-alcohol oxidase, glucose oxidase, methanol oxidase, pyranose oxidase, cellobiose dehydrogenase and pyranose dehydrogenase families was performed. The curated sequences were subjected to an analysis of their evolutionary relationships, followed by estimation of gene duplication/ reduction history during fungal evolution. Second, the molecular structures of the near one hundred GMC oxidoreductases identified were modeled to gain insight into their structural variation and expected catalytic properties. In contrast to ligninolytic peroxidases, whose genes are present in all white-rot Polyporales genomes and absent from those of brown-rot species, the H 2 O 2 -generating oxidases are widely distributed in both fungal types. This indicates that the GMC oxidases provide H 2 O 2 for both ligninolytic peroxidase activity (in white-rot decay) and Fenton attack on cellulose (in brown-rot decay), after the transition between both decay patterns in Polyporales occurred.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Ferreira¹,

Carro²,

Serrano³

et al. 2015

Mycologia

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“…Extracellular fluid of Bjertcandera adusta [17,18] has both peroxidase and oxidase activity with veratryl alcohol. In that case two distinct enzymes are involved, lignin peroxidase and veratryl (aryl) alcohol oxidase.…”

Section: 4 Chemicalsmentioning

confidence: 99%

Evidence for a new extracellular peroxidase Manganese‐inhibited peroxidase from the white‐rot fungus Bjerkandera sp. BOS 55

1992

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A novel enzyme activity was detected in the extra~llular fluid of Bjerkandera sp. BOS 55. The purified enzyme could oxidiz~ ~veral compounds. such as Phenol red, 2,6-dimethoxyphenol (DMP), Poly R-478, ABTS and gualacol, ~ith HaO2 as an el~tron accepter. In contrast, veratryl alcohol was not a substrate. This enzyme also had the capacity to oxidize DMP in the absence of H~O~. With some substrata, a strong inhibition of the peroxidative activiq, by Mn:" was observed. Phenol red oxidation was inhibited by 84% with only I mM of this metal ion. B~aur~ DMP oxidation by this enzyme is only slightly inhibited by Mn a,, this substrate should not be used in assays to detect manganese peroxidas¢. The enzyme is tentatively named 'Mangan~-Inhibited Peroxida~¢'.

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“…Several phenol derivatives of wood components and wood-biodegradation products have been shown to reduce Fe III and Cu II Aguiar and Ferraz, 2007 , and extracts from wood colonized by brown-rot and white-rot fungi have Fe III -reducing activity Goodell et al, 2006 . These Fe III -reducing compounds could participate in Fenton reactions to provide Fe II that is coupled with H 2 O 2 production by the fungi Kelly and Reddy, 1986;Kersten and Kirk, 1987;Guillén et al, 1990;Muheim et al, 1990 . Fe IIIreducing activity and catechol concentrations have been detected in wood extracts biotreated with C. subvermispora; however, wood extracts from undecayed samples had the highest reductive activity Aguiar et al, 2006.…”

Section: Discussionmentioning

confidence: 99%

Presence of Extracellular NAD<sup>+</sup> and NADH in Cultures of Wood-Degrading Fungi

et al. 2015

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Our previous studies indicated that extracellular glycoproteins produced by some white-rot and brown-rot basidiomycetous fungi reduce Fe(III) to Fe(II) and O 2 to H 2 O 2 and produce hydroxyl radicals. The continuous generation of hydroxyl radicals requires a constant supply of O 2 and an electron donor for the reduction of oxidized forms of the glycoproteins to the reduced forms. However, electron donors for this reaction, such as NADH, have not been identified. In this study, the amounts of the extracellular pyridine coenzymes, NAD and NADH, were measured in agar cultures of four white-rot fungi, one brown-rot fungus, and three soft-rot fungi. The sums of NAD and NADH detected in wood-containing cultures of all five basidiomycetes were greater than those in glucose cultures. The amounts of NAD were higher than those of NADH in all wood-containing cultures except that of Irpex lacteus, and NAD was greater than NADH in all glucose cultures except that of Fomitopsis palustris. Significant amounts of pyridine coenzymes were present in glucose and wood-containing cultures of the three soft-rot fungi. The non-wood-degrading fungus, Penicillium funiculosum, did not produce NAD or NADH in either glucose or wood-containing cultures. The extracellular pyridine coenzyme levels were relatively high compared to the rates of extracellular hydroxyl radical generation in wood-degrading fungal cultures. Thus, white-, brown-, and soft-rot fungi produce pyridine coenzymes that could serve as electron donors for the production of hydroxyl radicals during wood degradation.Key words White-rot fungi / Brown-rot fungi / Soft-rot fungi / Hydroxyl radical / NAD and NADH.

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An extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta

Cited by 98 publications

References 15 publications

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Evidence for a new extracellular peroxidase Manganese‐inhibited peroxidase from the white‐rot fungus Bjerkandera sp. BOS 55

Presence of Extracellular NAD<sup>+</sup> and NADH in Cultures of Wood-Degrading Fungi

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