作者: Edwin van Bloois , Daniel E. Torres Pazmiño , Remko T. Winter , Marco W. Fraaije
DOI: 10.1007/S00253-009-2369-X
关键词: Sequence alignment 、 Thermophile 、 Biochemistry 、 Enzyme 、 Dye decolorizing peroxidase 、 Heme 、 Periplasmic space 、 Bacterial genome size 、 Peroxidase 、 Biology
摘要: DyP-type peroxidases comprise a novel superfamily of heme-containing which is unrelated to the superfamilies known and only few members have been characterized in some detail. Here, we report identification characterization peroxidase (TfuDyP) from thermophilic actinomycete Thermobifida fusca. Biochemical recombinant enzyme showed that it monomeric, heme-containing, thermostable, Tat-dependently exported peroxidase. TfuDyP not active as dye-decolorizing also accepts phenolic compounds aromatic sulfides. In fact, able catalyze enantioselective sulfoxidations, type reaction has reported before for peroxidases. Site-directed mutagenesis was used determine role two conserved residues. D242 crucial catalysis while H338 represents proximal heme ligand essential incorporation. A genome database analysis revealed are frequently found bacterial genomes they extremely rare other organisms. Most homologs potential cytosolic enzymes, suggesting metabolic roles different dye degradation. conclusion, detailed biochemical here contributes significantly our understanding these enzymes further emphasizes their biotechnological potential.