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Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum.

ABSTRACT: 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.

SUBMITTER: Lohkamp B

PROVIDER: S-EPMC2150923 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum.

Lohkamp Bernhard B Andersen Birgit B Piskur Jure J Dobritzsch Doreen D

Acta crystallographica. Section F, Structural biology and crystallization communications 20051216 Pt 1

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, w ...[more]

PMID: 16511257

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