title: Crystallization and X-ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri.
abstract: Dihydropyrimidinase (EC 3.5.2.2) catalyzes the second step in the reductive pathway of pyrimidine degradation, the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri diffracting to 2.6 A at a synchrotron-radiation source have been obtained by the hanging-drop vapour-diffusion method. They belong to space group P2(1) (unit-cell parameters a = 91.0, b = 73.0, c = 161.4 A, beta = 91.4 degrees), with one homotetramer per asymmetric unit.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. doreen.dobritzsch@mbb.ki.se
authors.forename: Doreen
authors.initials: D
authors.lastname: Dobritzsch
authors.forename: Birgit
authors.initials: B
authors.lastname: Andersen
authors.forename: Jure
authors.initials: J
authors.lastname: Piskur
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D012440:Saccharomyces / Q000201:enzymology*; D014835:Volatilization; D014961:X-Ray Diffraction
chemical_list: D000581:Amidohydrolases; C020047:dihydropyrimidinase