Independent evolution of four heme peroxidase superfamilies

@inproceedings{Zmock2015IndependentEO,
  title={Independent evolution of four heme peroxidase superfamilies},
  author={Marcel Z{\'a}mock{\'y} and Stefan Hofbauer and I. Richard Schaffner and Bernhard Gasselhuber and Andrea Nicolussi and Monika Soudi and Katharina Franziska Pirker and Paul G Furtm{\"u}ller and Christian Obinger},
  booktitle={Archives of biochemistry and biophysics},
  year={2015}
}
Four heme peroxidase superfamilies (peroxidase-catalase, peroxidase-cyclooxygenase, peroxidase-chlorite dismutase and peroxidase-peroxygenase superfamily) arose independently during evolution, which differ in overall fold, active site architecture and enzymatic activities. The redox cofactor is heme b or posttranslationally modified heme that is ligated by either histidine or cysteine. Heme peroxidases are found in all kingdoms of life and typically catalyze the one- and two-electron oxidation… CONTINUE READING