Abstract
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 homooligomeric 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.
| Original language | English |
|---|---|
| Pages (from-to) | 142-146 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 406 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 1997 Apr 7 |
Bibliographical note
Funding Information:We thank Dr. Rosalind Kim for her advise and participation in the preparation of the manuscript. We gratefully acknowledge the support of Korea Institute of Science and Technology and a grant from Ministry of Science and Technology, Korea. The work of S.-H. Kim was supported by US Department of Energy (DOE-AC03-76S00098).
Keywords
- Aquifex
- Hyperthermophile
- Superoxide dismutase
- Thermostability
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
