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

B Lohkamp, Birgit Andersen, Jure Piskur, D Dobritzsch

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1 Citation (SciVal)

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 angstrom 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 angstrom and one molecule in the asymmetric unit.
Original languageEnglish
Pages (from-to)36-38
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications
Volume62
Issue number1
DOIs
Publication statusPublished - 2006

Subject classification (UKÄ)

  • Biological Sciences

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