Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum.
Dihydropyrimidinase (EC 3.5.2.2) is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 A resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 A and one molecule in the asymmetric unit.
Lohkamp
Bernhard
B
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Andersen
Birgit
B
Piskur
Jure
J
Dobritzsch
Doreen
D
D000581:Amidohydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004023:Dictyostelium / Q000201:enzymology*; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D015800:Protozoan Proteins; D011994:Recombinant Proteins; D000581:Amidohydrolases; C020047:dihydropyrimidinase