Active site plasticity in D-amino acid oxidase: a crystallographic analysis.

@article{Todone1997ActiveSP,
  title={Active site plasticity in D-amino acid oxidase: a crystallographic analysis.},
  author={F Todone and Maria Antonietta Vanoni and Andrea Mozzarelli and Martino Bolognesi and Alessandro Coda and Bruno Curti and Andrea Mattevi},
  journal={Biochemistry},
  year={1997},
  volume={36 19},
  pages={5853-60}
}
D-Amino acid oxidase (DAAO) is the prototype of the flavin-containing oxidases. It catalyzes the oxidative deamination of various D-amino acids, ranging from D-Ala to D-Trp. We have carried out the X-ray analysis of reduced DAAO in complex with the reaction product imino tryptophan (iTrp) and of the covalent adduct generated by the photoinduced reaction of the flavin with 3-methyl-2-oxobutyric acid (kVal). These structures were solved by combination of 8-fold density averaging and least-squares… CONTINUE READING