Sullivan F X, Shames S L, Walsh C T
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Biochemistry. 1989 Jun 13;28(12):4986-92. doi: 10.1021/bi00438a013.
The cloned trypanothione reductase gene from Trypanosoma congolense has been expressed in Escherichia coli to a level of 1% of the soluble protein. This has allowed facile purification and initial characterization of the reductase, and it appears by all criteria to be a representative member of the trypanothione reductase family. Most importantly, it shows the same exclusive substrate specificity for trypanothione over glutathione characteristic of other trypanothione reductases examined to date. The availability of the pure, cloned, sequenced reductase from T. congolense makes this enzyme a good target for structure/function studies and trypanocidal inhibitor design.
从刚果锥虫克隆的锥虫硫醇还原酶基因已在大肠杆菌中表达，表达水平达到可溶性蛋白的1%。这使得该还原酶易于纯化并进行初步表征，而且从各方面标准来看，它似乎是锥虫硫醇还原酶家族的代表性成员。最重要的是，与迄今检测的其他锥虫硫醇还原酶一样，它对锥虫硫醇具有相同的对谷胱甘肽的专一性底物特异性。来自刚果锥虫的纯的、已克隆和测序的还原酶的可得性，使得这种酶成为结构/功能研究和杀锥虫抑制剂设计的良好靶点。
