THERMAL DISASSEMBLY OF PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX FROM BACILLUS-STEAROTHERMOPHILUS

Citation
Y. Hiromasa et al., THERMAL DISASSEMBLY OF PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX FROM BACILLUS-STEAROTHERMOPHILUS, Bioscience, biotechnology, and biochemistry, 58(10), 1994, pp. 1904-1905
Citations number
13
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
58
Issue
10
Year of publication
1994
Pages
1904 - 1905
Database
ISI
SICI code
0916-8451(1994)58:10<1904:TDOPMC>2.0.ZU;2-T
Abstract
Thermostabilities of component enzymes in the pyruvate dehydrogenase c omplex from Bacillus stearothermophilus decreased in the order lipoami de dehydrogenase, lipoate acetyltransferase, and pyruvate decarboxylas e (E1). Fluorescence of an extrinsic 8-amino-1-naphthalenesulfonate (A NS) increased with inactivation of E1. The thermal denaturation of the enzymes resulted in disassembly of the complex. E1 was involved in a resulting aggregate of the complex. The interaction between ANS and de natured E1 accounted for an increase in fluorescence.