caa a22 4500 397556489 CHVBK 20180308164803.0 cr unu---uuuuu 161202e199609 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021454 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021454 2-Oxoacid:Ferredoxin Oxidoreductase from the Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7 [Elektronische Daten] [Qian Zhang, Toshio Iwasaki, Takayoshi Wakagi, Tairo Oshima] The purified 2-oxoacid:ferredoxin oxidoreductase of a thermoacidophilic and aerobic crenarchaeote, Sulfolobus sp. strain 7, consists of 70-kDa α and 37-kDa β subunits, and contains one thiamine pyrophosphate (TPP), one [4Fe-4S]2+,1+ cluster, and two magnesium atoms per αβ structure. It exhibits a broad substrate specificity toward 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate, and pyruvate. The gene encoding the archaeal oxidoreductase was cloned, and the two open reading frames encoding the α (632 amino acids) and β subunits (305 amino acids), respectively, were sequenced. Careful sequence alignment revealed several consensus motifs of this enzyme family, as well as possible cofactor binding residues of the Sulfolobus enzyme. This new structural information also indicates that (i) several genetic fusions and reorganization of the early, possibly αβγαβγδ-type enzyme similar to those from hyperthermophiles have taken place during evolution of the 2-oxo-acid:ferredoxin (flavodoxin) oxidoreductase superfamily, which might have occurred in different ways in early aerobic archaea and early anaerobic bacteria, and that (ii) enzymes with different subunit compositions should have an essentially similar catalytic mechanism with one TPP and at least one [4Fe-4S] cluster as the minimal set of redox centers. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence archaea (archaebacteria) nationallicence evolution nationallicence 2-oxoacid:ferredoxin oxidoreductase nationallicence primary structure nationallicence Sulfolobus nationallicence Zhang Qian Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut Iwasaki Toshio Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut Wakagi Takayoshi Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut Oshima Tairo Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut The Journal of Biochemistry Oxford University Press 120/3(1996-09), 587-599 0021-924X 120:3<587 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021454 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021454 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zhang Qian Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut NATIONALLICENCE 700 1- Iwasaki Toshio Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut NATIONALLICENCE 700 1- Wakagi Takayoshi Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut NATIONALLICENCE 700 1- Oshima Tairo Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 226 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/3(1996-09), 587-599 0021-924X 120:3<587 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford