嗜热栖热菌中热稳定邻氨基苯甲酸磷酸核糖基转移酶的纯化、表征及结晶
Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus.
作者信息
Ivens A, Mayans O, Szadkowski H, Wilmanns M, Kirschner K
机构信息
Institut für Biochemie der Universität zu Köln, Germany; EMBL-Hamburg Outstation, Hamburg, Germany.
出版信息
Eur J Biochem. 2001 Apr;268(8):2246-52. doi: 10.1046/j.1432-1327.2001.02102.x.
Anthranilate phosphoribosyltransferase (TrpD; EC 2.4.2.18) from the hyperthermophilic archaeon Sulfolobus solfataricus (ssTrpD) was expressed in Escherichia coli, purified and crystallized. Analytical gel permeation chromatography revealed a homodimeric composition of the enzyme. The steady-state kinetic characteristics suggest tight binding of the substrate anthranilic acid and efficient catalysis at the physiological growth temperature of S. solfataricus. Crystals of ssTrpD diffract to better than 2.6 A resolution and preliminary X-ray characterization was carried out. The crystals are suitable for structure determination.
来自嗜热古菌嗜热栖热菌（Sulfolobus solfataricus）的邻氨基苯甲酸磷酸核糖基转移酶（TrpD；EC 2.4.2.18，即ssTrpD）在大肠杆菌中表达、纯化并结晶。分析型凝胶渗透色谱显示该酶为同型二聚体结构。稳态动力学特征表明底物邻氨基苯甲酸与酶紧密结合，并在嗜热栖热菌的生理生长温度下能高效催化反应。ssTrpD晶体的衍射分辨率优于2.6 Å，并进行了初步的X射线表征。这些晶体适合进行结构测定。
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