Pyrophosphate hydrolysis in the extremely halophilic archaeon Haloarcula japonica is catalyzed by a single enzyme with a broad ionic strength range

Extremophiles ◽  
2017 ◽  
Vol 21 (3) ◽  
pp. 471-477 ◽  
Author(s):  
Satoshi Wakai ◽  
Akihiro Abe ◽  
Sotaro Fujii ◽  
Kaoru Nakasone ◽  
Yoshihiro Sambongi
Keyword(s):  
Ionic Strength ◽  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon ◽  
Pyrophosphate Hydrolysis ◽  
Single Enzyme

scholarly journals Identification of carotenoids from the extremely halophilic archaeon Haloarcula japonica

2014 ◽  
Vol 5 ◽  
Author(s):  
Rie Yatsunami ◽  
Ai Ando ◽  
Ying Yang ◽  
Shinichi Takaichi ◽  
Masahiro Kohno ◽  
...  
Keyword(s):  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon

Purification and partial characterization of cell surface glycoprotein from extremely halophilic archaeon Haloarcula japonica strain TR-1

1995 ◽  
Vol 17 (7) ◽  
pp. 705-706 ◽  
Author(s):  
Satoshi Nakamura ◽  
Shin Mizutani ◽  
Hiromichi Wakai ◽  
Hiroshi Kawasaki ◽  
Rikizo Aono ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Glycoprotein ◽  
Partial Characterization ◽  
Halophilic Archaeon ◽  
Cell Surface Glycoprotein ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon

scholarly journals Molecular cloning of transducer gene hjtB from extremely halophilic archaeon Haloarcula japonica

2005 ◽  
Vol 49 (1) ◽  
pp. 315-316
Author(s):  
Takayuki Kosaka ◽  
Takatoshi Ozawa ◽  
Rie Yatsunami ◽  
Toshiaki Fukui ◽  
Satoshi Nakamura
Keyword(s):  
Molecular Cloning ◽  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon

Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica

2021 ◽  
Author(s):  
Shintaro Nagaoka ◽  
Noriko Sugiyama ◽  
Rie Yatsunami ◽  
Satoshi Nakamura
Keyword(s):  
Analytical Ultracentrifugation ◽  
Maximum Activity ◽  
Oxidative Decarboxylation ◽  
Halophilic Archaeon ◽  
Leucine Biosynthesis ◽  
First Report ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon ◽  
Isopropylmalate Dehydrogenase

Abstract 3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 M KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH.

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