scholarly journals Molecular cloning of A1-ATPase gene from extremely halophilic archaeon Haloarcula japonica strain TR-1

1999 ◽  
Vol 42 (1) ◽  
pp. 75-76 ◽  
Author(s):  
R. Yatsunami ◽  
M. Iwamoto ◽  
K. lhara ◽  
S. Nakamura
Keyword(s):  
Molecular Cloning ◽  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Atpase Gene ◽  
Extremely Halophilic Archaeon ◽  
A1 Atpase

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

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

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.

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
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