TAILIEUCHUNG - Báo cáo khoa học: Importance of the gating segment in the substrate-recognition loop of pyranose 2-oxidase

Pyranose 2-oxidase fromTrametes multicoloris a 270 kDa homotetrameric enzyme that participates in lignocellulose degradation by wood-rotting fungi and oxidizes a variety of aldopyranoses present in lignocellulose to 2-ketoaldoses. | Importance of the gating segment in the substrate-recognition loop of pyranose 2-oxidase Oliver Spadiut1 Tien-Chye Tan1 2 Ines Pisanelli3 Dietmar Haltrich3 and Christina Divne1 2 1 KTH Biotechnology Royal institute of Technology Stockholm Sweden 2 Department of MedicalBiochemistry and Biophysics Karolinska Institutet Stockholm Sweden 3 Food Biotechnology Laboratory Department of Food Science and Technology BOKU - University of NaturalResources and Applied Life Sciences Vienna Austria Keywords active-site loop alanine-scanning mutagenesis crystal structure pyranose 2-oxidase site-saturation mutagenesis Correspondence C. Divne KTH Biotechnology Royal institute of Technology Albanova Roslagstullsbacken 21 SE-106 91 Stockholm Sweden Fax 46 8 5537 8468 Tel 46 8 5537 8296 E-mail divne@ or D. Haltrich Food Biotechnology Laboratory Department of Food Science and Technology BOKU - University of NaturalResources and Applied Life Sciences A-1190 Vienna Austria Fax 43 1 47654 6251 Tel 43 1 47654 6140 E-mail These authors contributed equally to this work Database The atomic coordinates and structure factors for the models are available in the Protein Data Bank database under the accession numbers 3K4J H450Q 3K4K F454N 3K4L F454N2fg 3K4M Y456W2FG and 3K4N F454A S455A Y456A Received 22 February 2010 revised 2 May 2010 accepted 6 May 2010 doi Pyranose 2-oxidase from Trametes multicolor is a 270 kDa homotetrameric enzyme that participates in lignocellulose degradation by wood-rotting fungi and oxidizes a variety of aldopyranoses present in lignocellulose to 2-ketoaldoses. The active site in pyranose 2-oxidase is gated by a highly conserved conformationally degenerate loop residues 450-461 with a conformer ensemble that can accommodate efficient binding of both electron-donor substrate sugar and electron-acceptor substrate oxygen or quinone compounds relevant to the sequential reductive and oxidative .

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