首页>
外国专利>
Genetically Engineered Arginine Deiminase Modified by Site-Directed Mutagenesis
Genetically Engineered Arginine Deiminase Modified by Site-Directed Mutagenesis
展开▼
机译:定点诱变修饰的基因工程精氨酸脱亚氨酶。
展开▼
页面导航
摘要
著录项
相似文献
摘要
A genetically engineered arginine deiminase reconstructed by site-directed mutagenesis belongs to the technical field of genetic engineering technology. Its amino acid sequence is shown as SEQ ID No. 1. In the amino acid sequence of the arginine deiminase reconstructed by site-directed mutagenesis, glycine at position 264 is mutated to proline, compared to an amino acid sequence of native arginine deiminase. Compared with wild type enzyme, the effective pH range effect of the mutated arginine deiminase according to the present invention is broadened to a certain extent, and especially a good enzyme activity is achieved at physiological pH 7.4. With the broadening of the effective pH effect range, the mutant enzyme still has higher stability under the condition of pH 5.5-7.5. Therefore, the problem that the arginine deiminase generally is low in enzymatic activity and short in half-life in vivo under physiological conditions in clinical application for tumor therapy is solved, and a good condition for using the enzyme and an encoding gene thereof for clinical treatment is created.
展开▼
机译:通过定点诱变重建的基因工程精氨酸脱亚氨酶属于基因工程技术领域。其氨基酸序列示为SEQ ID No.1。在通过定点诱变重建的精氨酸脱亚氨酶的氨基酸序列中,与天然精氨酸脱亚氨酶的氨基酸序列相比,位置264处的甘氨酸突变为脯氨酸。与野生型酶相比,根据本发明的突变的精氨酸脱亚氨酶的有效pH范围作用在一定程度上扩大了,特别是在生理pH 7.4下获得了良好的酶活性。随着有效pH作用范围的扩大,突变酶在pH 5.5-7.5的条件下仍具有较高的稳定性。因此,解决了在临床上用于肿瘤治疗的生理条件下,精氨酸脱亚氨酶通常在体内酶活性低,半衰期短的问题,为将该酶及其编码基因用于临床治疗提供了良好的条件。被建造。
展开▼