Thermally induced changes of lipoate acetyltransferase inner core isolated from the Bacillus stearothermophilus pyruvate dehydrogenase complex.
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.
Aso
Y
Y
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan. yaso@agr.kyushu-u.ac.jp
Nakajima
A
A
Meno
K
K
Ishiguro
M
M
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*
D003470:Culture Media; D011768:Pyruvate Dehydrogenase Complex; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D019791:Guanidine