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