Biochemical characterization of a low salt-adapted extracellular protease from the extremely halophilic archaeon Halococcus salifodinae

2021 ◽  
Vol 176 ◽  
pp. 253-259
Author(s):  
Jing Hou ◽  
Xue-Meng Yin ◽  
Yang Li ◽  
Dong Han ◽  
Bu Lü ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Extracellular Protease ◽  
Halophilic Archaeon ◽  
Low Salt ◽  
Extremely Halophilic Archaeon

Biochemical characterization of an extracellular polyextremophilic α-amylase from the halophilic archaeon Halorubrum xinjiangense

Extremophiles ◽  
2013 ◽  
Vol 17 (4) ◽  
pp. 677-687 ◽  
Author(s):  
Mahsa Moshfegh ◽  
Ahmad Reza Shahverdi ◽  
Gholamreza Zarrini ◽  
Mohammad Ali Faramarzi
Keyword(s):  
Biochemical Characterization ◽  
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.

scholarly journals Gene Analysis, Expression, and Characterization of an Intracellular α-Amylase from the Extremely Halophilic Archaeon Haloarcula japonica

2013 ◽  
Vol 77 (2) ◽  
pp. 281-288 ◽  
Author(s):  
Masahiko ONODERA ◽  
Rie YATSUNAMI ◽  
Wataru TSUKIMURA ◽  
Toshiaki FUKUI ◽  
Kaoru NAKASONE ◽  
...  
Keyword(s):  
Gene Analysis ◽  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon

Characterization of a GlgC homolog from extremely halophilic archaeon Haloarcula japonica

2021 ◽  
Author(s):  
Rin Sueda ◽  
Kento Yoshida ◽  
Masahiko Onodera ◽  
Toshiaki Fukui ◽  
Rie Yatsunami ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Glycogen Synthesis ◽  
Recombinant Enzyme ◽  
Halophilic Archaeon ◽  
Haloarcula Japonica ◽  
Extremely Halophilic Archaeon

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.

scholarly journals Identification and Characterization of gshA, a Gene Encoding the Glutamate-Cysteine Ligase in the Halophilic Archaeon Haloferax volcanii

2009 ◽  
Vol 191 (16) ◽  
pp. 5196-5204 ◽  
Author(s):  
Liron Malki ◽  
Michaela Yanku ◽  
Ilya Borovok ◽  
Gerald Cohen ◽  
Moshe Mevarech ◽  
...  
Keyword(s):  
Previous Analysis ◽  
Halophilic Archaea ◽  
Haloferax Volcanii ◽  
Halophilic Archaeon ◽  
Gene Encoding ◽  
Glutamate Cysteine Ligase ◽  
Extremely Halophilic Archaeon ◽  
Identification And Characterization

ABSTRACT Halophilic archaea were found to contain in their cytoplasm millimolar concentrations of γ-glutamylcysteine (γGC) instead of glutathione. Previous analysis of the genome sequence of the archaeon Halobacterium sp. strain NRC-1 has indicated the presence of a sequence homologous to sequences known to encode the glutamate-cysteine ligase GshA. We report here the identification of the gshA gene in the extremely halophilic archaeon Haloferax volcanii and show that H. volcanii gshA directs in vivo the synthesis and accumulation of γGC. We also show that the H. volcanii gene when expressed in an Escherichia coli strain lacking functional GshA is able to restore synthesis of glutathione.

Sign in / Sign up

Export Citation Format

Share Document