Results 161 to 170 of about 13,977 (211)
Groundwater Microbial Diversity Associated With Icelandic Basaltic Subsurface Environments. [PDF]
Bas-Lorillot J +11 more
europepmc +1 more source
The mechanics of a continuous self-assembling s urface-layer aids cell division in an archaeon
Foo S +4 more
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A defined cultivation medium for Sulfolobus acidocaldarius.
Journal of Biotechnology, 2019The thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius is an important model organism for Archaea and genetic systems are well established. To date, the organism is routinely cultivated on complex media based on protein hydrolysates and no common ...
Julian Quehenberger +5 more
semanticscholar +3 more sources
Metabolism of Pentose Sugars in the Hyperthermophilic Archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius [PDF]
We have previously shown that the hyperthermophilic archaeon, Sulfolobus solfataricus, catabolizes d-glucose and d-galactose to pyruvate and glyceraldehyde via a non-phosphorylative version of the Entner-Doudoroff pathway. At each step, one enzyme is active with both C6 epimers, leading to a metabolically promiscuous pathway.
Tobias Fuhrer +2 more
exaly +3 more sources
The Prefoldin of the Crenarchaeon Sulfolobus solfataricus
Protein & Peptide Letters, 2008Prefoldin is a hetero-hexameric ATP-independent chaperone, shared by eukaryotes and archaea, which binds non-native proteins preventing them from aggregation. We report the identification and characterization in vivo and in vitro of the first prefoldin from a crenarchaeon, the hyperthermophile Sulfolobus solfataricus.
Ciaramella M +4 more
openaire +8 more sources
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 +4 more
openaire +6 more sources
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 +4 more
openaire +6 more sources
Current Opinion in Biotechnology, 2019
Archaea dominate extreme habitats and possess unique cellular and metabolic properties with novel or modified metabolic pathways and unusual enzymes. Thermoacidophilic Sulfolobus species and their thermo(acido)philic enzymes gained special attention due ...
Larissa Schocke, C. Bräsen, B. Siebers
semanticscholar +1 more source
Archaea dominate extreme habitats and possess unique cellular and metabolic properties with novel or modified metabolic pathways and unusual enzymes. Thermoacidophilic Sulfolobus species and their thermo(acido)philic enzymes gained special attention due ...
Larissa Schocke, C. Bräsen, B. Siebers
semanticscholar +1 more source
Carboxylase genes of Sulfolobus metallicus
Archives of Microbiology, 1999Carbon dioxide limitation of Sulfolobus metallicus resulted in increased cellular concentrations of polypeptides that were predicted to be biotin carboxylase and biotin carboxyl-carrier-protein components of a protein complex. These polypeptides were coeluted from a native polyacrylamide gel and were estimated at 19 and 59 kDa after separation by ...
N P, Burton, T D, Williams, P R, Norris
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