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Electrostatic interaction between two domains of isocitrate dehydrogenase from Thermus thermophilus is important for the catalytic function and protein stability
Author(s) -
Yaoi Takuro,
Hayashi-Iwasaki Yoko,
Oshima Tairo
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01243-4
Subject(s) - thermus thermophilus , thermostability , isocitrate dehydrogenase , chemistry , site directed mutagenesis , mutant , active site , mutagenesis , function (biology) , biochemistry , protein–protein interaction , enzyme , stereochemistry , biology , escherichia coli , microbiology and biotechnology , gene
The role of electrostatic interaction between Lys 96 and Glu 47 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 Glu 147 Gln mutant revealed that this interaction plays important roles in catalytic function and protein stability.