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

Författare:
  • B Lohkamp
  • Birgit Andersen
  • Jure Piskur (Professor)
  • D Dobritzsch
Publiceringsår: 2006
Språk: Engelska
Sidor: 36-38
Publikation/Tidskrift/Serie: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
Volym: 62
Nummer: 1
Dokumenttyp: Artikel
Förlag: Blackwell Publishing Ltd

Sammanfattning

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.

Disputation

Nyckelord

  • Chemistry

Övriga

Published
Yes
  • ISSN: 1744-3091

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