Results 161 to 170 of about 5,681 (181)

Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius

Extremophiles, 2016
Sulfolobus acidocaldarius, a hyperthermoacidophilic archaeon, possesses two β-decarboxylating dehydrogenase genes, saci_0600 and saci_2375, in its genome, which suggests that it uses these enzymes for three similar reactions in lysine biosynthesis through 2-aminoadipate, leucine biosynthesis, and the tricarboxylic acid cycle.
Takahashi, Kento, Nakanishi, Fumika, Tomita, Takeo, Akiyama, Nagisa, Lassak, Kerstin, Albers, Sonja Verena, Kuzuyama, Tomohisa, Nishiyama, Makoto   +7 more
openaire   +3 more sources

Membrane-bound ATPase of a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1985
The membranes of Sulfolobus, a thermoacidophilic archaebacterium showed two types of ATP hydrolyzing activity. One was that of a neutral ATPase at an optimum pH around 6.5. This enzyme was activated by 10 mM sulfate with a shift of optimum pH to 5.
T, Wakagi, T, Oshima
openaire   +2 more sources

A secY homologous gene in the crenarchaeon Sulfolobus acidocaldarius

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1995
The nucleotide sequence of an open reading frame, located upstream of the gene for adenylate kinase, was determined in the thermoacidophile crenarchaeon Sulfolobus acidocaldarius. Data bank searches identified the sequence as a secY homologous gene. The DNA derived protein sequence of total 463 amino acids contains 10 hydrophobic domains.
T, Kath, G, Schäfer
openaire   +2 more sources

Molecule and Gene of Sulfolobus acidocaldarius ATPase

1990
A novel ATPase (Sul-ATPase) was solubilized from membranes of an archaebacterium, Sulfolobus acidocaldarius, by washing with a buffer containing EDTA. Enzymatic characteristics of this ATPase are distinctly different from F1-ATPase and resemble eukaryotic endomembrane H+-ATPase.
Kimitoshi Denda, Jin Konishi, Kyoko Hajiro, Tairo Oshima, Takayasu Date, Masasuke Yoshida   +5 more
openaire   +1 more source

Purification and characterization of NADH oxidase from the archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus

Biotechnology and Applied Biochemistry, 1996
The enzyme NADH oxidase (EC 1.6.99.3) has been isolated from the two thermoacidophilic archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus and characterized. In both organisms the enzyme oxidizes specifically beta‐NADH in the presence of molecular oxygen and requires the presence of a flavin cofactor, showing a high specificity for FAD.
MASULLO, Mariorosario, RAIMO G, DELLO RUSSO A, BOCCHINI V, BANNISTER JV   +4 more
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Chromatin Immunoprecipitation Assay in the Hyperthermoacidophilic Crenarchaeon, Sulfolobus acidocaldarius

2017
Chromatin immunoprecipitation (ChIP) is a powerful method used for identifying genome-wide DNA-protein interactions in vivo. A large number of essential intracellular processes such as DNA replication, transcription regulation, chromatin stability, and others are all dependent on protein interactions with DNA.
Kun, Wang, Ann-Christin, Lindås
openaire   +2 more sources

AmyA contributes to the glycogen synthesis in Sulfolobus acidocaldarius

International Journal of Biological Macromolecules
Glycogen, an α-1,4 linked glucose polymer with α-1,6 linked branches, accumulates in Sulfolobus acidocaldarius in granular form and contributes to stress resistance. While the glg operon responsible for glycogen metabolism has been studied, the gene responsible for branch formation remained elusive.
Areum, Lee, Nahyun, Park, Chihong, Song, Jaeho, Cha   +3 more
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DNA polymerase from Sulfolobus acidocaldarius

Journal of Molecular Biology, 1989
Samia Salhi, Christiane Elie, Patrick Forterre, Anni-Marie de Recondo, Jean-Michel Rossignol   +4 more
openaire   +1 more source

Biosynthesis of Caldariellaquinone in Sulfolobus acidocaldarius

2014
Ph. D.
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Characterization of RNAse J in Sulfolobus acidocaldarius

2012
In Archaea the exosome is a 3´-to- 5´ RNA processing and degaradation ma-chinery. However, recent studies identified a 5´-to- 3´ exoribonuclease termed Sso-RNAse J in the crenarchaeum Sulfolobus solfataricus (Sso). Here, we characterized a Sso-RNase J orthologue in Sulfolobus acidocaldarius (SacI-RNase J), which comprises typical signature motifs of ...
openaire   +1 more source