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Crystallization and X-ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri
Karolinska Institutet. (Molecular Structural Biology)
2005 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 61, no Pt 4, 359-362 p.Article in journal (Refereed) Published
Abstract [en]

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 beta-amino acids. Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri diffracting to 2.6 A at a synchrotron-radiation source have been obtained by the hanging-drop vapour-diffusion method. They belong to space group P2(1) (unit-cell parameters a = 91.0, b = 73.0, c = 161.4 A, beta = 91.4 degrees), with one homotetramer per asymmetric unit.

Place, publisher, year, edition, pages
2005. Vol. 61, no Pt 4, 359-362 p.
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Structural Biology
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URN: urn:nbn:se:uu:diva-214437DOI: 10.1107/S174430910500610XISI: 000232293200006PubMedID: 16511040OAI: oai:DiVA.org:uu-214437DiVA: diva2:684944
Available from: 2014-01-08 Created: 2014-01-08 Last updated: 2017-12-06Bibliographically approved

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Dobritzsch, Doreen

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