Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis, crystallization and preliminary X-ray diffraction studies of the enzyme.

@article{Nielsen1996PurificationAC,
  title={Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis, crystallization and preliminary X-ray diffraction studies of the enzyme.},
  author={Flemming Seier Nielsen and Paul Rowland and Sine Larsen and Kaj Jensen},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 5},
  pages={852-6}
}
Lactococcus lactis is the only organism known to contain two dihydroorotate dehydrogenases, i.e., the A- and B-forms. In this paper, we report the overproduction, purification, and crystallization of dihydroorotate dehydrogenase A. In solution, the enzyme is bright yellow. It is a dimer of subunits (34 kDa) that contain one molecule of flavin mononucleotide each. The enzyme shows optimal function in the pH range 7.5-9.0. It is specific for L-dihydroorotate as substrate and can use… CONTINUE READING
7 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-7 of 7 extracted citations

Similar Papers

Loading similar papers…