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Protein Engineering, Vol. 14, No. 2, 81-84, February 2001
© 2001 Oxford University Press

Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures

Raita Hirose1, Toshiharu Suzuki1,2, Hideaki Moriyama1,3, Takao Sato1, Akihiko Yamagishi4, Tairo Oshima4 and Nobuo Tanaka1,5

1 Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226-8501 and 4 School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi 14–32–1, Hachioji,Tokyo 192-0392, Japan

Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases (IPMDH; EC 1.1.1.85) produced mutant enzymes which adapt to low temperatures. These mutants had higher activity at lower temperatures than the wild-type enzyme without losing high thermostability. Here we report three structures of the mutants of Thermus thermophilus IPMDH determined by X-ray diffraction which was adapted to a low-temperature environment. Two of them have unstable coenzyme binding states and the other one probably has a stable substrate binding state. The present research suggests that the adaptation is correlated with the binding of either coenzyme or the substrate.


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