Open AccessCrystallization and X‐ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri
Author(s) -
Dobritzsch Doreen,
Andersen Birgit,
Piškur Jure
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910500610x
Subject(s) - homotetramer , crystallization , chemistry , crystallography , saccharomyces cerevisiae , hydrolysis , yeast , pyrimidine , x ray , saccharomyces , single crystal , stereochemistry , biochemistry , organic chemistry , physics , protein subunit , gene , quantum mechanics
Dihydropyrimidinase (EC 3.5.2.2) catalyzes the second step in the reductive pathway of pyrimidine degradation, the hydrolysis of 5,6‐dihydrouracil and 5,6‐dihydrothymine to the corresponding N‐carbamylated β‐amino acids. Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri diffracting to 2.6 Å at a synchrotron‐radiation source have been obtained by the hanging‐drop vapour‐diffusion method. They belong to space group P 2 1 (unit‐cell parameters a = 91.0, b = 73.0, c = 161.4 Å, β = 91.4°), with one homotetramer per asymmetric unit.