Crystallization and preliminary X-ray study of pig liver dihydropyrimidine dehydrogenase

被引：7

作者：

Dobritzsch, D ^{[1
]}

Persson, K ^{[1
]}

Schneider, G ^{[1
]}

Lindqvist, Y ^{[1
]}

机构：

[1] Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444900015250

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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 Angstrom, beta = 96.1 degrees), with two homodimers per asymmetric unit.

引用

页码：153 / 155

页数：3

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