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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt 1):36-8. doi: 10.1107/S174430910503976X. Epub 2005 Dec 16.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Dictyostelium / enzymology*
  • Molecular Sequence Data
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / isolation & purification*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Protozoan Proteins
  • Recombinant Proteins
  • Amidohydrolases
  • dihydropyrimidinase