Crystallization and preliminary X-ray study of pig liver dihydropyrimidine dehydrogenase.
Dihydropyrimidine dehydrogenase catalyzes the first and rate-limiting reaction in pyrimidine catabolism. The enzyme contains one FMN, one FAD and four Fe-S clusters per subunit of 1025 amino acids as prosthetic groups. It is also the major determinant of bioavailability and toxicity of 5-fluorouracil, a chemotherapeutic agent widely used in the treatment of solid tumors. Crystals of this enzyme diffracting to at least 2.5 A have been obtained by the hanging-drop vapour-diffusion method and belong to space group P2(1) (unit-cell parameters a = 82.0, b = 159.3, c = 163.6 A, beta = 96.1 degrees ), with two homodimers per asymmetric unit.
Dobritzsch
D
D
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Persson
K
K
Schneider
G
G
Lindqvist
Y
Y
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D042943:Dihydrouracil Dehydrogenase (NADP); D008099:Liver / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013552:Swine
D011994:Recombinant Proteins; D010088:Oxidoreductases; D042943:Dihydrouracil Dehydrogenase (NADP)