We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Pressure adaptation of 3-isopropylmalate dehydrogenase from an extremely piezophilic bacterium is attributed to a single amino acid substitution.
- Authors
Hamajima, Yuki; Watanabe, Nobuhisa; Nagae, Takayuki; Ohmae, Eiji; Kato-Yamada, Yasuyuki; Kato, Chiaki
- Abstract
3-Isopropylmalate dehydrogenase (IPMDH) from the extreme piezophile Shewanella benthica (SbIPMDH) is more pressure-tolerant than that from the atmospheric pressure-adapted Shewanella oneidensis (SoIPMDH). To understand the molecular mechanisms of this pressure tolerance, we analyzed mutated enzymes. The results indicate that only a single mutation at position 266, corresponding to Ala (SbIPMDH) and Ser (SoIPMDH), essentially affects activity under higher-pressure conditions. Structural analyses of SoIPMDH suggests that penetration of three water molecules into the cleft around Ser266 under high-pressure conditions could reduce the activity of the wild-type enzyme; however, no water molecule is observed in the Ala266 mutant.
- Subjects
BAROPHILIC bacteria; HIGH pressure biology; DEHYDROGENASES; MOLECULAR microbiology; DEPTH-area-duration (Hydrometeorology)
- Publication
Extremophiles, 2016, Vol 20, Issue 2, p177
- ISSN
1431-0651
- Publication type
Article
- DOI
10.1007/s00792-016-0811-4