A novel enzyme, L-tryptophan oxidase, from a basidiomycete, Coprinus sp. SF-1: purification and characterization.

@article{Furuya2000ANE,
  title={A novel enzyme, L-tryptophan oxidase, from a basidiomycete, Coprinus sp. SF-1: purification and characterization.},
  author={Y{\^u}ji Furuya and Hiroshi Sawada and Toshikatsu Hirahara and Kousuke Ito and Takashi Ohshiro and Yoshikazu Izumi},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2000},
  volume={64 7},
  pages={1486-93}
}
A basidiomycete, Coprinus sp. SF-1, was found to produce an L-Trp-oxidizing enzyme by screening from the culture collection of our laboratory. After solubilization by 1 M NaSCN from the particulate fraction of disrupted cells of the strain, the enzyme was purified about 76-fold to essential homogeneity. The enzyme had a molecular mass of about 420 kDa and the subunit molecular mass was 68 kDa. The enzyme contained 1 mol of non-covalently bound FAD per mol of the subunit. It catalyzed the… CONTINUE READING