DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.

@article{Sugano2007DyPAU,
  title={DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases.},
  author={Yasushi Sugano and Riichi Muramatsu and Atsushi Ichiyanagi and Takao Sato and Makoto Shoda},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 50},
  pages={36652-8}
}
DyP, a unique dye-decolorizing enzyme from the fungus Thanatephorus cucumeris Dec 1, has been classified as a peroxidase but lacks homology to almost all other known plant peroxidases. The primary structure of DyP shows moderate sequence homology to only two known proteins: the peroxide-dependent phenol oxidase, TAP, and the hypothetical peroxidase, cpop21. Here, we show the first crystal structure of DyP and reveal that this protein has a unique tertiary structure with a distal heme region… CONTINUE READING

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