title: Thermally induced changes of lipoate acetyltransferase inner core isolated from the Bacillus stearothermophilus pyruvate dehydrogenase complex.
abstract: Incubation at 70 degrees C converted the Bacillus stearothermophilus lipoate acetyltransferase inner core into an unidentified active molecular form, X, yielding an inactive aggregate. The core and X showed similar thermostabilities, but they were different in the recovery of enzyme activity after incubation with 1.2-2.0 M guanidine hydrochloride and its subsequent removal; the core was hardly recovered, but X was well recovered.
authors.affiliation: Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan. yaso@agr.kyushu-u.ac.jp
authors.forename: Y
authors.initials: Y
authors.lastname: Aso
authors.forename: A
authors.initials: A
authors.lastname: Nakajima
authors.forename: K
authors.initials: K
authors.lastname: Meno
authors.forename: M
authors.initials: M
authors.lastname: Ishiguro
mesh_terms: D000123:Acetyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D003470:Culture Media; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000187:drug effects / Q000201:enzymology* / Q000254:growth & development; D019791:Guanidine / Q000494:pharmacology; D006361:Heating; D008027:Light; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*
chemical_list: D003470:Culture Media; D011768:Pyruvate Dehydrogenase Complex; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D019791:Guanidine