Characterization of thermostable native alkaline phosphatase from an aerobic hyperthermophilic archaeon, Aeropyrum pernix K1

2007 ◽  
Vol 74 (1) ◽  
pp. 107-112 ◽  
Author(s):  
Is Helianti ◽  
Takako Okubo ◽  
Yasutaka Morita ◽  
Eiichi Tamiya
Keyword(s):  
Alkaline Phosphatase ◽  
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

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

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

Characterization of a novel moderate-substrate specificity amino acid racemase from the hyperthermophilic archaeon Thermococcus litoralis

2021 ◽  
Author(s):  
Ryushi Kawakami ◽  
Chinatsu Kinoshita ◽  
Tomoki Kawase ◽  
Mikio Sato ◽  
Junji Hayashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Enzyme Stability ◽  
Hyperthermophilic Archaea ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
Aminobutyrate Aminotransferase ◽  
Chaperone Protein ◽  
Amino Acid Racemase

Abstract The amino acid sequence of the OCC_10945 gene product from the hyperthermophilic archaeon Thermococcus litoralis DSM5473, originally annotated as γ-aminobutyrate aminotransferase, is highly similar to that of the uncharacterized pyridoxal 5ʹ-phosphate (PLP)-dependent amino acid racemase from Pyrococcus horikoshii. The OCC_10945 enzyme was successfully overexpressed in Escherichia coli by co-expression with a chaperone protein. The purified enzyme demonstrated PLP-dependent amino acid racemase activity primarily toward Met and Leu. Although PLP contributed to enzyme stability, it only loosely bound to this enzyme. Enzyme activity was strongly inhibited by several metal ions, including Co2+ and Zn2+, and non-substrate amino acids such as l-Arg and l-Lys. These results suggest that the underlying PLP-binding and substrate recognition mechanisms in this enzyme are significantly different from those of the other archaeal and bacterial amino acid racemases. This is the first description of a novel PLP-dependent amino acid racemase with moderate substrate specificity in hyperthermophilic archaea.

scholarly journals Sequence and characterization of the human intestinal alkaline phosphatase gene.

1988 ◽  
Vol 263 (24) ◽  
pp. 12011-12019 ◽  
Author(s):  
P S Henthorn ◽  
M Raducha ◽  
T Kadesch ◽  
M J Weiss ◽  
H Harris
Keyword(s):  
Alkaline Phosphatase ◽  
Intestinal Alkaline Phosphatase

scholarly journals Isolation and characterization of a small intestinal surfactant-like particle containing alkaline phosphatase and other digestive enzymes

1989 ◽  
Vol 264 (34) ◽  
pp. 20614-20619 ◽  
Author(s):  
R Eliakim ◽  
K DeSchryver-Kecskemeti ◽  
L Nogee ◽  
W.F. Stenson ◽  
D.H. Alpers
Keyword(s):  
Alkaline Phosphatase ◽  
Digestive Enzymes ◽  
Isolation And Characterization ◽  
Small Intestinal
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