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

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Author

  • B Lohkamp
  • Birgit Andersen
  • Jure Piskur
  • D Dobritzsch

Summary, in English

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.

Publishing year

2006

Language

English

Pages

36-38

Publication/Series

Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Volume

62

Issue

1

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences

Status

Published

ISBN/ISSN/Other

  • ISSN: 2053-230X