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Total records: 126
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[ 2016 ] Maté D, Alcalde M Laccase: a multi-purpose biocatalyst at the forefront of biotechnology Microbial Biotechnol., doi: 10.1111/1751-7915.12422

[ 2016 ] Mathieu Y, Piumi F, Valli R, Carro J, Ferreira P, Faulds CB, Record E Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass Appl. Environ. Microbiol., 82: 2411-2423

[ 2016 ] Molina-Espeja P, Cañellas M, Plou FJ, Hofrichter M, Lucas F, Guallar V, Alcalde M Synthesis of 1-Naphthol by a Natural Peroxygenase engineered by Directed Evolution ChemBioChem, 17: 341-349

[ 2016 ] Molina-Espeja P, Viña-Gonzalez J, Gomez-Fernandez BJ, Martin-Diaz J, García-Ruiz E, Alcalde M Beyond the outer limits of nature by directed evolution Biotechnol. Adv., 34: 754-767

[ 2016 ] Ni Y, Fernandez-Fueyo E, Gomez Baraibar A, Ullrich R, Hofrichter M, Yanase H, Alcalde M, van Berkel WJ, Hollmann F Peroxygenase-Catalyzed Oxyfunctionalization Reactions Promoted by the Complete Oxidation of Methanol Angew. Chem. Int. Ed., 55: 798-801

[ 2016 ] Olmedo A, Aranda C, del Río JC, Kiebist J, Scheibner K, Martínez AT, Gutiérrez A From Alkanes to Carboxylic Acids: Terminal Oxygenation by a Fungal Peroxygenase Angew. Chem. Int. Ed., 55: 12248-12251

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 thePycnoporus cinnabarinusCIRM 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 inAspergillus niger Based on the enzyme's activity and specificity, it was assigned to the glucose dehydrogenases (PcinnabarinusGDH [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 fromPleurotus 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 andPcAAQO3). Structural comparison ofPcAAQO homology models withP. eryngiiAAO 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 ofPcAAQOs to reduce radical intermediates generated by laccase fromP. cinnabarinuswas demonstrated, shedding light on the ligninolytic system of this fungus.

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