Electrostatic interaction between two domains of isocitrate dehydrogenase from Thermus thermophilus is important for the catalytic function and protein stability

FEBS Letters

Yaoi, Takuro¹  Hayashi-Iwasaki, Yoko¹  Oshima, Tairo¹ 

[1] Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-03, Japan

关键词: Active site;    Thermostability;    Site-directed mutagenesis;    Thermophilic enzyme;   

DOI  :  10.1016/S0014-5793(96)01243-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The role of electrostatic interaction between Lys⁹⁶ and Glu⁴⁷ of isocitrate dehydrogenase from Thermus thermophilus was investigated by site-directed mutagenesis. These two residues are located near the active site and involved in the interdomain interaction. Analyses of the catalytic properties and thermostability of the Glu¹⁴⁷Gln mutant revealed that this interaction plays important roles in catalytic function and protein stability.

【 授权许可】

Unknown