Characterization of a GlgC homolog from extremely halophilic archaeon Haloarcula japonica

Author(s):  
Rin Sueda ◽  
Kento Yoshida ◽  
Masahiko Onodera ◽  
Toshiaki Fukui ◽  
Rie Yatsunami ◽  
...  

ABSTRACT Glycogen synthesis in bacteria is mainly organized by the products of glgB, glgC, and glgA genes comprising the widely known glg operon. On the genome of extremely halophilic archaeon Haloarcula japonica, there was a gene cluster analogous to the bacterial glg operon. In this study, we focused on a GlgC homolog of Ha. japonica, and its recombinant enzyme was prepared and characterized. The enzyme showed highest activity toward GTP and glucose-1-phosphate as substrates in the presence of 2.6 m KCl and predicted to be work as “GDP-glucose pyrophosphorylase” in Ha. japonica.

Author(s):  
Shintaro Nagaoka ◽  
Noriko Sugiyama ◽  
Rie Yatsunami ◽  
Satoshi Nakamura

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.


2013 ◽  
Vol 77 (2) ◽  
pp. 281-288 ◽  
Author(s):  
Masahiko ONODERA ◽  
Rie YATSUNAMI ◽  
Wataru TSUKIMURA ◽  
Toshiaki FUKUI ◽  
Kaoru NAKASONE ◽  
...  

2014 ◽  
Vol 5 ◽  
Author(s):  
Rie Yatsunami ◽  
Ai Ando ◽  
Ying Yang ◽  
Shinichi Takaichi ◽  
Masahiro Kohno ◽  
...  

2005 ◽  
Vol 49 (1) ◽  
pp. 315-316
Author(s):  
Takayuki Kosaka ◽  
Takatoshi Ozawa ◽  
Rie Yatsunami ◽  
Toshiaki Fukui ◽  
Satoshi Nakamura

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