An active-site mutation enhances the catalytic activity of the yeast Cryptococcus humicola d-aspartate oxidase

@inproceedings{Takahashi2009AnAM,
  title={An active-site mutation enhances the catalytic activity of the yeast Cryptococcus humicola d-aspartate oxidase},
  author={Shouji Takahashi and S Matsumoto and Kazuhiro Maruyama and Ayaka Wakaizumi and Katsumasa Abe and Yoshio Kera and Ryo-hei Yamada},
  year={2009}
}
Abstract d -Aspartate oxidase (ChDDO) of the yeast Cryptococcus humicola has a much higher specificity and reactivity to d -aspartate than those from other sources, making it useful for some applications in science and fine-chemical industries. We constructed a three-dimensional model of ChDDO and compared it with the crystal structure of a yeast d -amino acid oxidase. The comparison showed an arginine residue positioned at 243 of ChDDO that was possibly involved in the substrate recognition… CONTINUE READING