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Crystallization and preliminary X-ray study of pig liver dihydropyrimidine dehydrogenase
Karolinska Institutet. (Molecular Structural Biology)
2001 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 57, no Pt 1, 153-155 p.Article in journal (Refereed) Published
Abstract [en]

Dihydropyrimidine dehydrogenase catalyzes the first and rate-limiting reaction in pyrimidine catabolism. The enzyme contains one FMN, one FAD and four Fe-S clusters per subunit of 1025 amino acids as prosthetic groups. It is also the major determinant of bioavailability and toxicity of 5-fluorouracil, a chemotherapeutic agent widely used in the treatment of solid tumors. Crystals of this enzyme diffracting to at least 2.5 A have been obtained by the hanging-drop vapour-diffusion method and belong to space group P2(1) (unit-cell parameters a = 82.0, b = 159.3, c = 163.6 A, beta = 96.1 degrees ), with two homodimers per asymmetric unit.

Place, publisher, year, edition, pages
2001. Vol. 57, no Pt 1, 153-155 p.
National Category
Structural Biology
URN: urn:nbn:se:uu:diva-214445DOI: 10.1107/S0907444900015250ISI: 000166157700022PubMedID: 11134942OAI: oai:DiVA.org:uu-214445DiVA: diva2:684839
Available from: 2014-01-08 Created: 2014-01-08 Last updated: 2014-01-15Bibliographically approved

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Dobritzsch, Doreen
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