Andreotti G, Tutino M L, Sannia G, Marino G, Cubellis M V
Department of Organic and Biological Chemistry, University of Naples, Federico II, Italy.
Biochim Biophys Acta. 1994 Oct 19;1208(2):310-5. doi: 10.1016/0167-4838(94)90118-x.
Indole-3-glycerol-phosphate synthase, a thermophilic and thermostable enzyme from the archaeon Sulfolobus solfataricus, was purified and characterized. The sequence of the thermophilic enzyme was compared to the sequence of a homologous mesophilic enzyme from Escherichia coli. The secondary structure of the thermophilic enzyme was predicted taking into account the patterns of hydropathy, chain flexibility and amphipathicity and the CD spectrum. From this analysis it turned out that indole-3-glycerol-phosphate synthase from S. solfataricus can be considered a model for studying thermostable TIM-barrel enzymes. Some peculiarities of the amino-acid sequence of indole-3-glycerol-phosphate synthase from S. solfataricus are discussed in relation to the thermostability of the enzyme.
对来自古菌嗜热栖热菌的吲哚 - 3 - 甘油磷酸合酶（一种嗜热且耐热的酶）进行了纯化和表征。将该嗜热酶的序列与来自大肠杆菌的同源嗜温酶的序列进行了比较。考虑到亲水性、链柔性、两亲性模式以及圆二色光谱，对嗜热酶的二级结构进行了预测。通过该分析发现，嗜热栖热菌的吲哚 - 3 - 甘油磷酸合酶可被视为研究耐热TIM桶状酶的模型。结合该酶的热稳定性，讨论了嗜热栖热菌吲哚 - 3 - 甘油磷酸合酶氨基酸序列的一些特性。
