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Cloning and expression of superoxide dismutase from Aquifex pyrophilus , a hyperthermophilic bacterium
Author(s) -
Lim Jae-Hwan,
Yu Yeon Gyu,
Choi In-Geol,
Ryu Jae-Ryeon,
Ahn Byung-Yoon,
Kim Sung-Hou,
Han Ye Sun
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00262-7
Subject(s) - aquifex aeolicus , escherichia coli , biochemistry , superoxide dismutase , thermophile , bacteria , cloning (programming) , peptide sequence , chemistry , gene , biology , microbiology and biotechnology , enzyme , genetics , computer science , programming language
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.