Purification and properties of dihydropterin oxidase from Drosophila melanogaster.

@article{Unnasch1982PurificationAP,
  title={Purification and properties of dihydropterin oxidase from Drosophila melanogaster.},
  author={Thomas R. Unnasch and Gavin M. Brown},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 23},
  pages={14211-6}
}
The enzyme dihydropterin oxidase has been purified to apparent homogeneity from the fruit fly Drosophila melanogaster. This enzyme uses a variety of 2-amino-4-oxo-7,8-dihydropteridine compounds as substrates, including 2-amino-4-oxo-7,8-dihydropteridine (called dihydropterin), Km = 0.11 microM; 6-lactoyl-7,8-dihydropterin, Km = 1.80 microM; and 7,8-dihydrobiopterin, Km = 1.25 microM. The products in each case are the corresponding fully oxidized compounds 2-amino-4-oxopteridine, oxidized 6… CONTINUE READING