Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium

A superoxide dismutase ( SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homo-oligo...

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Bibliographic Details
Published in:FEBS letters 1997-04, Vol.406 (1), p.142-146
Main Authors: Lim, Jae-Hwan, Yu, Yeon Gyu, Choi, In-Geol, Ryu, Jae-Ryeon, Ahn, Byung-Yoon, Kim, Sung-Hou, Han, Ye Sun
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aquifex
Aquifex pyrophilus
Base Sequence
Cloning, Molecular
Cytochrome c Group - metabolism
DNA, Recombinant
Enzyme Stability
Escherichia coli
Gram-Negative Aerobic Bacteria - enzymology
Gram-Negative Aerobic Bacteria - genetics
Hot Temperature
Hyperthermophile
Molecular Sequence Data
Superoxide dismutase
Superoxide Dismutase - genetics
Superoxide Dismutase - isolation & purification
Superoxide Dismutase - metabolism
Thermostability
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Summary:A superoxide dismutase ( SOD) gene of Aquifex pyrophilus, a marine hyperthermophilic bacterium, was cloned, sequenced, expressed in Escherichia coli, and its gene product characterized. This is the first SOD from a hyperthermophilic bacterium that has been cloned. It is an iron-containing homo-oligomeric protein with a monomeric molecular mass of 24.2 kDa. The DNA-derived amino acid sequence is more similar to those of known Mn- and Fe-SODs from thermophilic archaea than of Cu, Zn-SODs. The metal binding residues found in all SOD sequences from different species are also conserved in A. pyrophilus SOD. The protein is biochemically active only as an oligomer and is resistant to thermal denaturation.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00262-7