Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus

1997 ◽  
Vol 168 (5) ◽  
pp. 412-420 ◽  
Author(s):  
Ida Helene Steen ◽  
Torleiv Lien ◽  
Nils-Kåre Birkeland
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Archaeoglobus Fulgidus ◽  
Hyperthermophilic Archaeon ◽  
Phylogenetic Characterization

Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus

Extremophiles ◽  
2001 ◽  
Vol 5 (5) ◽  
pp. 323-332 ◽  
Author(s):  
Servé Kengen ◽  
Floris Bikker ◽  
Wilfred Hagen ◽  
Willem Vos ◽  
John Oost
Keyword(s):  
Archaeoglobus Fulgidus ◽  
Hyperthermophilic Archaeon ◽  
Catalase Peroxidase

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.

DETECTION AND PHYLOGENETIC CHARACTERIZATION OF HEPATITIS E VIRUS GENOTYPE 3 IN A CAPTIVE WILD BOAR IN THAILAND

2012 ◽  
Vol 43 (3) ◽  
pp. 640-644 ◽  
Author(s):  
Anuwat Wiratsudakul ◽  
Ladawan Sariya ◽  
Phirom Prompiram ◽  
Siriporn Tantawet ◽  
Duangkhamol Suraruangchai ◽  
...  
Keyword(s):  
Wild Boar ◽  
Hepatitis E Virus ◽  
Hepatitis E ◽  
Genotype 3 ◽  
Virus Genotype ◽  
Phylogenetic Characterization
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