Lim, JH Yu, YG Choi, IG Ryu, JR Ahn, BY Kim, SH Han, YS 2024-01-21T18:33:16Z 2024-01-21T18:33:16Z 2021-09-01 1997-04-07 0014-5793 https://pubs.kist.re.kr/handle/201004/143846 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. (C) 1997 Federation of European Biochemical Societies. English ELSEVIER SCIENCE BV CRYSTAL-STRUCTURE ESCHERICHIA-COLI GENE-EXPRESSION MANGANESE RESOLUTION PROTEINS ENZYMES REVEALS Cloning and expression of superoxide dismutase from Aquifex pyrophilus, a hyperthermophilic bacterium Article 10.1016/S0014-5793(97)00262-7 1 FEBS LETTERS, v.406, no.1-2, pp.142 - 146 FEBS LETTERS 406 1-2 142 146 scie scopus A1997WT54800032 2-s2.0-0030914069 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article CRYSTAL-STRUCTURE ESCHERICHIA-COLI GENE-EXPRESSION MANGANESE RESOLUTION PROTEINS ENZYMES REVEALS hyperthermophile superoxide dismutase thermostability Aquifex