Electrostatic interaction between two domains of isocitrate dehydrogenase from Thermus thermophilus is important for the catalytic function and protein stability.
The role of electrostatic interaction between Lys96 and Glu147 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.
Yaoi
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T
Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Hachioji, Japan.
Hayashi-Iwasaki
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Y
Oshima
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D000595:Amino Acid Sequence; D002384:Catalysis; D004563:Electrochemistry; D004795:Enzyme Stability; D018698:Glutamic Acid / Q000737:chemistry; D005973:Glutamine / Q000737:chemistry; D006358:Hot Temperature; D007521:Isocitrate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D016963:Thermus thermophilus / Q000201:enzymology*
D005973:Glutamine; D018698:Glutamic Acid; D007521:Isocitrate Dehydrogenase; D008239:Lysine