Purification and characterization of a veratryl alcohol oxidase enzyme from the lignin degrading basidiomycete Pleurotus ostreatus

Sannia, Giovanni; Limongi, Paola; Cocca, Ennio; Buonocore, Francesco; Nitti, Gianpaolo; Giardina, Paola

doi:10.1016/0304-4165(91)90190-r

Cited by 98 publications

(56 citation statements)

References 24 publications

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“…Consequently, we propose a novel cooperation between laccase and MnP according to the scheme shown in Fig. 8 (13,16,19,27,31,41,42). Concerning biotechnological applications, laccase offers a simple and convenient alternative to supply peroxidases with H 2 O 2 , because laccases will become available at an economically feasible scale.…”

Section: Mnmentioning

confidence: 99%

“…Extracellular H 2 O 2 is required as a substrate for ligninolytic peroxidases. Extracellular enzymes like aryl alcohol oxidase (31) and glyoxal oxidase (19) produce H 2 O 2 . This compound is also formed upon oxidation of hydroquinones by ligninolytic enzymes and autoxidation of the resulting semiquinones concomitantly reducing O 2 to superoxide anion radical (13,27 …”

mentioning

confidence: 99%

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Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase

Schlößer

Höfer²

2002

Appl Environ Microbiol

188

115

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Section: Mnmentioning

confidence: 99%

mentioning

confidence: 99%

Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase

Schlößer

Höfer²

2002

Appl Environ Microbiol

188

115

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“…They were first described in Polystictus versicolor (5). AAO activity was later detected in different fungi, including Pleurotus species (6)(7)(8)(9), Fusarium solani (10), Rigidoporus microporus (synonym, Fomes lignosus) (11), Bjerkandera adusta (12,13), and Botrytis cinerea (14). The simultaneous production of AAO and lignin peroxidase (LiP) in B. adusta (15) and of AAO and versatile peroxidase in Pleurotus cultures (16) supports AAO involvement in lignin degradation.…”

mentioning

confidence: 99%

Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass

Mathieu

Piumi

Valli

et al. 2016

Appl Environ Microbiol

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Auxiliary activities family 3 subfamily 2 (AA3_2) from the CAZy database comprises various functions related to ligninolytic enzymes, such as fungal aryl alcohol oxidases (AAO) and glucose oxidases, both of which are flavoenzymes. The recent study of the Pycnoporus cinnabarinus CIRM BRFM 137 genome combined with its secretome revealed that four AA3_2 enzymes are secreted during biomass degradation. One of these AA3_2 enzymes, scf184803.g17, has recently been produced heterologously in Aspergillus niger. Based on the enzyme's activity and specificity, it was assigned to the glucose dehydrogenases (P. cinnabarinus GDH [PcGDH]). Here, we analyze the distribution of the other three AA3_2 enzymes (scf185002.g8, scf184611.g7, and scf184746.g13) to assess their putative functions. These proteins showed the highest homology with aryl alcohol oxidase from Pleurotus eryngii. Biochemical characterization demonstrated that they were also flavoenzymes harboring flavin adenine dinucleotide (FAD) as a cofactor and able to oxidize a wide variety of phenolic and nonphenolic aryl alcohols and one aliphatic polyunsaturated primary alcohol. Though presenting homology with fungal AAOs, these enzymes exhibited greater efficiency in reducing electron acceptors (quinones and one artificial acceptor) than molecular oxygen and so were defined as aryl-alcohol: quinone oxidoreductases (AAQOs) with two enzymes possessing residual oxidase activity (PcAAQO2 and PcAAQO3). Structural comparison of PcAAQO homology models with P. eryngii AAO demonstrated a wider substrate access channel connecting the active-site cavity to the solvent, explaining the absence of activity with molecular oxygen. Finally, the ability of PcAAQOs to reduce radical intermediates generated by laccase from P. cinnabarinus was demonstrated, shedding light on the ligninolytic system of this fungus.A uxiliary activities (AA) are a widespread group of catalytic modules involved in plant cell wall degradation. They were first introduced in 2013 into the carbohydrate-active enzymes (CAZy [www.cazy.org]) database (1). This AA class encompasses and extends an earlier classification dedicated to fungal ligninolytic enzymes and comprises 10 families, some of which have subfamilies (2). The AA family group enzymes possess the potential ability to help the original carbohydrate-active enzymes gain access to the carbohydrates embedded in the plant cell wall. Lignin, the main noncarbohydrate structural component of plant cell walls, consists of an intricate network of aromatic compounds forming a strong, hydrophobic, insoluble barrier closing access to the carbohydrates. Microorganisms have therefore set up different strategies to either modify or degrade lignin as a first step to gain access to the carbohydrate moiety and convert it into an energy source (3).In this new AA classification, family AA3 belongs to the glucose-methanol-choline (GMC) oxidoreductase family first defined by Cavener (4). AA3 enzymes are flavoproteins containing a flavin adenine dinucleotide (FAD)-binding domai...

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“…The extracellular aryl-alcohol oxidases have an acidic pH optimum thereby oxidizing a variety of non-activated or methoxylated aromatic alcohols (Sannia et al, 1991 ;Guillen et al, 1992). In contrast, vanillyl-alcohol oxidase from P simplicissimum has a basic pH optimum and acts solely on 4-hydroxybenzyl alcohols (de Jong et al, 1992).…”

mentioning

confidence: 99%

Substrate Specificity of Flavin‐Dependent Vanillyl‐Alcohol Oxidase from Penicillium Simplicissimum

Fraaije¹,

Veeger²,

Berkel³

1995

European Journal of Biochemistry

131

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The substrate specificity of the flavoprotein vanillyl-alcohol oxidase from Penicillium simplicissimum was investigated. Vanillyl-alcohol oxidase catalyzes besides the oxidation of 4-hydroxybenzyl alcohols, the oxidative deamination of 4-hydroxybenzylamines and the oxidative demethylation of 4-(methoxymethy1)phenols. During the conversion of vanillylamine to vanillin, a transient intermediate, most probably vanillylimine, is observed.Vanillyl-alcohol oxidase weakly interacts with 4-hydroxyphenylglycoIs and a series of catecholamines. These compounds are converted to the corresponding ketones. Both enantiomers of (nor)epinephrine are substrates for vanillyl-alcohol oxidase, but the R isomer is preferred.Vanillyl-alcohol oxidase is most active with chavicol and eugenol. These 4-allylphenols are converted to coumaryl alcohol and coniferyl alcohol, respectively. Isotopic labeling experiments show that the oxygen atom inserted at the Cy atom of the side chain is derived from water. The 4-hydroxycinnamyl alcohol products and the substrate analog isoeugenol are competitive inhibitors of vanillyl alcohol oxidation.The binding of isoeugenol to the oxidized enzyme perturbs the optical spectrum of protein-bound FAD. pH-dependent binding studies suggest that vanillyl-alcohol oxidase preferentially binds the phenolate form of isoeugenol (pK,<6, 25°C). From this and the high pH optimum for turnover, a hydride transfer mechanism involving a p-quinone methide intermediate is proposed for the vanillyl-alcoholoxidase-catalyzed conversion of 4-allylphenols.Keywords: 4-allylphenols ; aromatic alcohol oxidase; covalently bound flavin; substrate specificity ; vanillin.Several fungi produce aryl-alcohol oxidases that are involved in the biodegradation of lignin, the most abundant aromatic biopolymer Abbreviations. Adrenalone, 3',4'-dihydroxy-2-methylaminoacetophenone; 4-allylanisole, 4-methoxy-allylbenzene; anisyl alcohol, 4-methoxybenzyl alcohol ; chavicol, 4-allylphenol ; cinnamyl alcohol, 3-phenyl-2-propene-1-01; coniferyl alcohol, 4-hydroxy-3-methoxycinnamyl alcohol ; coumaryl alcohol, 4-hydroxycinnamyl alcohol; epinephrine, 3,4-dihydroxy-u-(methylaminomethyl)benzyl alcohol (adrenalin); eugenol, 4-allyl-2-methoxyphenol ; homovanillyl alcohol, 4-hydroxy-3-methoxyphenethyl alcohol ; isoeugenol, 2-methoxy-4-propenylphenol; isosafrole, 1,2-(methylenedioxy)-4-propenylbenzene; metanephrine, 4-hydroxy-3-methoxy-a-(methylaminomethyl)benzyl alcohol; norepinephrine, a-(aminomethyl)-3,4-dihydroxybenzyl alcohol (noradrenalin); normetanephrine, n-(aminomethyl)-4-hydroxy-3-methoxybenzyl alcohol; octopamine, a-(aminornethyl)-4-hydroxybenzyl alcohol; safrole, 4-allyl-1,2-(methylenedioxy)benzene; synephrine, 4-hydroxy-a-(methylaminomethy1)benzyl alcohol; vanillyl alcohol, 4-hydroxy-3-methoxybenzyl alcohol ; vanillylamine, 4-hydroxy-3-methoxybenzylarnine ; vanillin, 4-hydroxy-3-methoxybenzaldehyde; veratryl alcohol, 3,4-dirnethoxybenzyl alcohol.

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Purification and characterization of a veratryl alcohol oxidase enzyme from the lignin degrading basidiomycete Pleurotus ostreatus

Cited by 98 publications

References 24 publications

Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase

Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase

Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass

Substrate Specificity of Flavin‐Dependent Vanillyl‐Alcohol Oxidase from Penicillium Simplicissimum

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Purification and characterization of a veratryl alcohol oxidase enzyme from the lignin degrading basidiomycete Pleurotus ostreatus

Cited by 98 publications

References 24 publications

Laccase-Catalyzed Oxidation of Mn 2+ in the Presence of Natural Mn 3+ Chelators as a Novel Source of Extracellular H 2 O 2 Production and Its Impact on Manganese Peroxidase

Laccase-Catalyzed Oxidation of Mn 2+ in the Presence of Natural Mn 3+ Chelators as a Novel Source of Extracellular H 2 O 2 Production and Its Impact on Manganese Peroxidase

Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass

Substrate Specificity of Flavin‐Dependent Vanillyl‐Alcohol Oxidase from Penicillium Simplicissimum

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Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase

Laccase-Catalyzed Oxidation of Mn ²⁺ in the Presence of Natural Mn ³⁺ Chelators as a Novel Source of Extracellular H ₂ O ₂ Production and Its Impact on Manganese Peroxidase