title: Characterization of a novel DyP-type peroxidase from Streptomyces avermitilis.
abstract: DyP-type peroxidases are a heme peroxidase family with unique properties whose members are widely distributed from prokaryotes to eukaryotes. DyP-type peroxidases are subdivided into class P, I and V based on structure-based sequence alignment. Class V enzymes possess degradation activities for anthraquinone dyes, and include extra sequences compared with class P and I. Class V enzymes are mainly found in fungi, with only two such proteins, AnaPX and DyP2, reported in bacteria. Here, we heterologously expressed, purified and biochemically characterized SaDyP2 protein, predicted to belong to class V. SaDyP2 was purified as a ∼50 kDa enzyme containing a heme cofactor and was found to oxidize the typical peroxidase substrates, ABTS and DMP. SaDyP2 was generally thermostable and exhibited a lower optimal pH, a feature typical of DyP-type peroxidases. It also degraded anthraquinone dyes, a specific substrate of DyP-type peroxidases, although the kcatfor SaDyP2 was lower than that for other class V enzymes. The Kmvalue of SaDyP2 for anthraquinone dye was similar to that of other enzymes of this class. Homology modeling revealed that the structure of SaDyP2 best fit that of class V enzymes.
authors.affiliation: Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-Ku, Tokyo 112-8681, Japan.
authors.forename: Kanako
authors.initials: K
authors.lastname: Sugawara
authors.affiliation: Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-Ku, Tokyo 112-8681, Japan.
authors.forename: Yuriko
authors.initials: Y
authors.lastname: Nishihashi
authors.affiliation: Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-Ku, Tokyo 112-8681, Japan.
authors.forename: Tomomi
authors.initials: T
authors.lastname: Narioka
authors.affiliation: Department of Bioresource and Environmental Sciences, Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555, Japan.
authors.forename: Toru
authors.initials: T
authors.lastname: Yoshida
authors.affiliation: Environmental Chemistry and Engineering, Interdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8503, Japan.
authors.forename: Mifumi
authors.initials: M
authors.lastname: Morita
authors.affiliation: Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-Ku, Tokyo 112-8681, Japan. Electronic address: suganoy@fc.jwu.ac.jp.
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Sugano
mesh_terms: D000595:Amino Acid Sequence; D000880:Anthraquinones / Q000378:metabolism; D004396:Coloring Agents / Q000378:metabolism; D004795:Enzyme Stability; D006418:Heme / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry / Q000145:classification* / Q000302:isolation & purification / Q000378:metabolism*; D016415:Sequence Alignment; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000880:Anthraquinones; D004396:Coloring Agents; D006418:Heme; D009195:Peroxidase
keywords: Anthraquinone degradation; Class V; DyP-type peroxidase; Streptomyces; Structure-based sequence alignment