Crystallization and X-ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri.
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.
Dobritzsch
Doreen
D
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. doreen.dobritzsch@mbb.ki.se
Andersen
Birgit
B
Piskur
Jure
J
D000581:Amidohydrolases / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D012440:Saccharomyces / Q000201:enzymology*; D014835:Volatilization; D014961:X-Ray Diffraction
D000581:Amidohydrolases; C020047:dihydropyrimidinase