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Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans.

Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K

Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

UDP-N-acetylglucosamine pyrophosphorylase (UAP) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine. UAP from Candida albicans was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals of the substrate and product complexes both diffract X-rays to beyond 2.3 A resolution using synchrotron radiation. The crystals of the substrate complex belong to the triclinic space group P1, with unit-cell parameters a = 47.77, b = 62.89, c = 90.60 A, alpha = 90.01, beta = 97.72, gamma = 92.88 degrees, whereas those of the product complex belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.95, b = 90.87, c = 94.88 A.

Published 4 December 2006 in Acta Crystallograph Sect F Struct Biol Cryst Commun, 62: 1206-8.
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