Characterization of native glutamate dehydrogenase from an aerobic hyperthermophilic archaeon Aeropyrum pernix K1

2001 ◽  
Vol 56 (3-4) ◽  
pp. 388-394 ◽  
Author(s):  
I. Helianti ◽  
Y. Morita ◽  
A. Yamamura ◽  
Y. Murakami ◽  
K. Yokoyama ◽  
...  
Keyword(s):  
Glutamate Dehydrogenase ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix

Purification and characterization of carbon monoxide dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix

2010 ◽  
Vol 76 (6) ◽  
pp. 999-1006 ◽  
Author(s):  
Hiroshi Nishimura ◽  
Yoshiko Nomura ◽  
Eri Iwata ◽  
Nozomi Sato ◽  
Yoshihiko Sako
Keyword(s):  
Carbon Monoxide ◽  
Carbon Monoxide Dehydrogenase ◽  
Purification And Characterization ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix

Glutamate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1: enzymatic characterization, identification of the encoding gene, and phylogenetic implications

Extremophiles ◽  
2000 ◽  
Vol 4 (6) ◽  
pp. 333-341 ◽  
Author(s):  
Mohammad W. Bhuiya ◽  
Haruhiko Sakuraba ◽  
Chizu Kujo ◽  
Naoki Nunoura-Kominato ◽  
Yutaka Kawarabayasi ◽  
...  
Keyword(s):  
Glutamate Dehydrogenase ◽  
Enzymatic Characterization ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Phylogenetic Implications ◽  
Encoding Gene

Crystallization and preliminary X-ray diffraction analysis of glutamate dehydrogenase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1

2002 ◽  
Vol 58 (8) ◽  
pp. 1338-1339 ◽  
Author(s):  
Mohammad W. Bhuiya ◽  
Hideaki Tsuge ◽  
Haruhiko Sakuraba ◽  
Kazunari Yoneda ◽  
Nobuhiko Katunuma ◽  
...  
Keyword(s):  
Diffraction Analysis ◽  
Glutamate Dehydrogenase ◽  
X Ray Diffraction ◽  
Hyperthermophilic Archaeon ◽  
X Ray ◽  
Aeropyrum Pernix

scholarly journals Characterization of a Novel Thermostable O-Acetylserine Sulfhydrylase from Aeropyrum pernix K1

2003 ◽  
Vol 185 (7) ◽  
pp. 2277-2284 ◽  
Author(s):  
Koshiki Mino ◽  
Kazuhiko Ishikawa
Keyword(s):  
Escherichia Coli ◽  
Rate Constant ◽  
Binding Motif ◽  
Phosphate Binding ◽  
Ph Optimum ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Synthetic Reaction

ABSTRACT An O-acetylserine sulfhydrylase (OASS) from the hyperthermophilic archaeon Aeropyrum pernix K1, which shares the pyridoxal 5′-phosphate binding motif with both OASS and cystathionine β-synthase (CBS), was cloned and expressed by using Escherichia coli Rosetta(DE3). The purified protein was a dimer and contained pyridoxal 5′-phosphate. It was shown to be an enzyme with CBS activity as well as OASS activity in vitro. The enzyme retained 90% of its activity after a 6-h incubation at 100°C. In the O-acetyl-l-serine sulfhydrylation reaction, it had a pH optimum of 6.7, apparent Km values for O-acetyl-l-serine and sulfide of 28 and below 0.2 mM, respectively, and a rate constant of 202 s−1. In the l-cystathionine synthetic reaction, it showed a broad pH optimum in the range of 8.1 to 8.8, apparent Km values for l-serine and l-homocysteine of 8 and 0.51 mM, respectively, and a rate constant of 0.7 s−1. A. pernix OASS has a high activity in the l-cysteine desulfurization reaction, which produces sulfide and S-(2,3-hydroxy-4-thiobutyl)-l-cysteine from l-cysteine and dithiothreitol.

scholarly journals Gene Expression and Characterization of a Third Type of Dye-LinkedL-Proline Dehydrogenase from the Aerobic Hyperthermophilic Archaeon,Aeropyrum pernix

2012 ◽  
Vol 76 (3) ◽  
pp. 589-593 ◽  
Author(s):  
Takenori SATOMURA ◽  
Yusuke HARA ◽  
Shin-ichiro SUYE ◽  
Haruhiko SAKURABA ◽  
Toshihisa OHSHIMA
Keyword(s):  
Gene Expression ◽  
Proline Dehydrogenase ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix
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