tailieunhanh - Báo cáo khoa học: Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma

We purified an extracellular pyranose dehydrogenase (PDH) from the basidiomycete fungusAgaricus xanthodermausing ammonium sulfate frac-tionation and ion-exchange and hydrophobic interaction chromatography. The native enzyme is a monomeric glycoprotein (5% carbohydrate) con-taining a covalently bound FAD as its prosthetic group. | ỊFEBS Journal Properties of pyranose dehydrogenase purified from the litter-degrading fungus Agaricus xanthoderma Magdalena Kujawa1 Jindrich Volc2 Petr Halada2 Petr Sedmera2 Christina Divne3 Christoph Sygmund1 Christian Leitner1 Clemens Peterbauer1 and Dietmar Haltrich1 1 Division of Food Biotechnology Department of Food Sciences and Technology BOKU - University of NaturalResources and Applied Life Sciences Vienna Austria 2 Institute of Microbiology Academy of Sciences of the Czech Republic Prague Czech Republic 3 Schoolof Biotechnology KTH Albanova University Center Stockholm Sweden Keywords covalent flavinylation lignocellulose degradation litter-degrading fungi pyranose dehydrogenase Correspondence D. Haltrich Department fur Lebensmittelwissenschaften und -technologie Universitat fur Bodenkultur Muthgasse 18 A-1190 Vienna Austria Fax 43 1 36006 6251 Tel 43 1 36006 6275 E-mail Website http Received 22 August 2006 revised 4 December 2006 accepted 7 December 2006 doi We purified an extracellular pyranose dehydrogenase PDH from the basidiomycete fungus Agaricus xanthoderma using ammonium sulfate fractionation and ion-exchange and hydrophobic interaction chromatography. The native enzyme is a monomeric glycoprotein 5 carbohydrate containing a covalently bound FAD as its prosthetic group. The PDH polypeptide consists of 575 amino acids and has a molecular mass of 65 400 Da as determined by MALDI MS. On the basis of the primary structure of the mature protein PDH is a member of the glucose-meth-anol-choline oxidoreductase family. We constructed a homology model of PDH using the 3D structure of glucose oxidase from Aspergillus niger as a template. This model suggests a novel type of bi-covalent flavinylation in PDH 9-S-cysteinyl 8-a-N3-histidyl FAD. The enzyme exhibits a broad sugar substrate tolerance oxidizing structurally different aldopyranoses including monosaccharides and .

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