title: Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans.
abstract: 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.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Maruyama
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Nishitani
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Nonaka
authors.forename: Akiko
authors.initials: A
authors.lastname: Kita
authors.forename: Takaaki A
authors.initials: TA
authors.lastname: Fukami
authors.forename: Toshiyuki
authors.initials: T
authors.lastname: Mio
authors.forename: Hisafumi
authors.initials: H
authors.lastname: Yamada-Okabe
authors.forename: Toshiko
authors.initials: T
authors.lastname: Yamada-Okabe
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D002176:Candida albicans / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D009713:Nucleotidyltransferases; C023226:UDPacetylglucosamine pyrophosphorylase