Journal
EXTREMOPHILES
Volume 5, Issue 3, Pages 183-192Publisher
SPRINGER-VERLAG
DOI: 10.1007/s007920100190
Keywords
Sulfolobus solfataricus; Archaea; amidase; signatured amidase; thermophiles
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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 first characterized archaeal amidase, is a monomer of 55,784 daltons, enantioselective, and active on 2- to 6-carbon aliphatic amides and on many aromatic amides, over the pH range 4-9 and at temperatures from 60 degrees to 95 degreesC. The S. solfataricus amidase belongs to the class of amidases that share a characteristic signature, GGSS(S/G)GS, located in the central region of the protein, and which show remarkable variability in their individual substrate specificities, can hydrolyze aliphatic or aromatic substrates, and share a large invariance of their primary structure.
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