Tutino M L, Tosco A, Marino G, Sannia G
Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Italy.
Biochem Biophys Res Commun. 1997 Jan 13;230(2):306-10. doi: 10.1006/bbrc.1996.5951.
The genes trpE and trpG of the hyperthermophilic archaeon Sulfolobus solfataricus, encoding the components I and II of anthranilate synthase, were cloned and co-expressed in Escherichia coli. The properties of the recombinant protein were determined and compared to those of the wild type complex. Gel filtration chromatography revealed an alpha2beta2 composition. The heteromeric enzyme is fully active above 85 degrees C and can be considered to be an "extremozyme" according to Adams et al.[1]. Sulfolobus solfataricus anthranilate synthase is subject to feedback inhibition by L-tryptophan even if it lacks the co-operativity that has been observed for all the other tetrameric anthranilate synthases.
嗜热古菌嗜热栖热菌（Sulfolobus solfataricus）中编码邻氨基苯甲酸合酶组分I和II的trpE和trpG基因被克隆，并在大肠杆菌中共同表达。测定了重组蛋白的性质，并与野生型复合物的性质进行了比较。凝胶过滤色谱显示其组成为α2β2。这种异源酶在85摄氏度以上具有完全活性，根据亚当斯等人[1]的定义，可被视为一种“极端酶”。即使嗜热栖热菌邻氨基苯甲酸合酶缺乏其他所有四聚体邻氨基苯甲酸合酶所具有的协同性，但它仍受L-色氨酸的反馈抑制。
