Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures |
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| Authors: | Hirose, Raita Suzuki, Toshiharu Moriyama, Hideaki Sato, Takao Yamagishi, Akihiko Oshima, Tairo Tanaka, Nobuo |
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| Affiliation: | 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 |
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| Abstract: | Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases(IPMDH; EC 1.1.1.85) produced mutant enzymes which adapt tolow temperatures. These mutants had higher activity at lowertemperatures than the wild-type enzyme without losing high thermostability.Here we report three structures of the mutants of Thermus thermophilusIPMDH determined by X-ray diffraction which was adapted to alow-temperature environment. Two of them have unstable coenzymebinding states and the other one probably has a stable substratebinding state. The present research suggests that the adaptationis correlated with the binding of either coenzyme or the substrate. |
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