Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 62(Pt 1): 36-8, 2006 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-16511257
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Protozoários
/
Dictyostelium
/
Amidoidrolases
Limite:
Animals
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article