| Avtor/Urednik | Lohkamp, Bernhard; Andersen, Birgit; Piškur, Jure; Dobritzsch, Doreen | |
| Naslov | Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum | |
| Tip | članek | |
| Vir | Acta Crystallogr Sect F Struct Biol Cryst Commun | |
| Vol. in št. | Letnik 62, št. Pt 1 | |
| Leto izdaje | 2006 | |
| Obseg | str. 36-8 | |
| Jezik | eng | |
| Abstrakt | 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. | |
| Deskriptorji | AMIDOHYDROLASES AMINO ACID SEQUENCE ANIMALS CRYSTALLIZATION CRYSTALLOGRAPHY, X-RAY DICTYOSTELIUM MOLECULAR SEQUENCE DATA PROTOZOAN PROTEINS RECOMBINANT PROTEINS |