Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus

We have cloned, sequenced, and overexpressed in Escherichia coli the amidase gene from the hyperthermophilic archaeon Sulfolobus solfataricus (strain MT4). The recombinant thermophilic protein was expressed as a fusion protein with an N-terminus six-histidine-residue affinity tag. The enzyme, the fi...

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Veröffentlicht in:	Extremophiles (Tokyo. Print) 2001-06, Vol.5 (3), p.183-192
Hauptverfasser:	SCOTTO D'ABUSCO, Anna, AMMENDOLA, Sergio, SCANDURRA, Roberto, POLITI, Laura
Format:	Artikel
Sprache:	eng
Schlagworte:	Amidohydrolases - chemistry Amidohydrolases - genetics Amidohydrolases - metabolism Amino Acid Sequence Bacteriology Base Sequence Biological and medical sciences Cloning, Molecular DNA, Archaeal - genetics Enzyme Activation - drug effects Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Genes, Archaeal Hydrogen-Ion Concentration Isoelectric Point Kinetics Metabolism. Enzymes Metals - pharmacology Microbiology Molecular Sequence Data Molecular Weight Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid Space life sciences Substrate Specificity Sulfolobus - enzymology Sulfolobus - genetics Temperature
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