DyP-type peroxidases comprise a novel heme peroxidase family.
Dye-decolorizing peroxidase (DyP) is produced by a basidiomycete (Thanatephorus cucumeris Dec 1) and is a member of a novel heme peroxidase family (DyP-type peroxidase family) that appears to be distinct from general peroxidases. Thus far, 80 putative members of this family have been registered in the PeroxiBase database (http://peroxibase.isbsib.ch/) and more than 400 homologous proteins have been detected via PSI-BLAST search. Although few studies have characterized the function and structure of these proteins, they appear to be bifunctional enzymes with hydrolase or oxygenase, as well as typical peroxidase activities. DyP-type peroxidase family suggests an ancient root compared with other general peroxidases because of their widespread distribution in the living world. In this review, firstly, an outline of the characteristics of DyP from T. cucumeris is presented and then interesting characteristics of the DyP-type peroxidase family are discussed.
Sugano
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Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, Japan. ysugano@res.titech.ac.jp
D000818:Animals; D001487:Basidiomycota / Q000201:enzymology*; D002711:Chloride Peroxidase; D030562:Databases, Protein; D006801:Humans; D006899:Mixed Function Oxygenases; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D010802:Phylogeny; D011487:Protein Conformation; D016415:Sequence Alignment
D006899:Mixed Function Oxygenases; D010544:Peroxidases; D002711:Chloride Peroxidase; C022333:peroxygenase