Thermally induced changes of lipoate acetyltransferase inner core isolated from the Bacillus stearothermophilus pyruvate dehydrogenase complex

Incubation at 70°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 incubatio...

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Published inBioscience, biotechnology, and biochemistry Vol. 65; no. 3; pp. 698 - 701
Main Authors Aso, Y. (Kyushu Univ., Fukuoka (Japan)), Nakajima, A, Meno, K, Ishiguro, M
Format Journal Article
LanguageEnglish
Published Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.03.2001
Japan Society for Bioscience Biotechnology and Agrochemistry
Oxford University Press
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Summary:Incubation at 70°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.
Bibliography:2001004009
F60
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ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.65.698