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

Raita Hirose, Toshiharu Suzuki, Hideaki Moriyama, Takao Sato, Akihiko Yamagishi, Tairo Oshima, Nobuo Tanaka

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Random mutagenesis on thermophilic 3-isopropylmalate dehydrogenases (IPMDH; EC 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.

Original languageEnglish (US)
Pages (from-to)81-84
Number of pages4
JournalProtein Engineering
Issue number2
StatePublished - 2001
Externally publishedYes


  • 3-isopropylmalate dehydrogenase
  • Cold-adapted mutants
  • Structural analysis
  • Thermal stability
  • Thermus thermophilus

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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