Thermostabilities of component enzymes in the pyruvate dehydrogenase complex from Bacillus stearothermophilus decreased in the order lipoamide dehydrogenase, lipoate acetyltransferase, and pyruvate decarboxylase (E1). Fluorescence of an extrinsic 8-amino-1-naphthalenesulfonate (ANS) 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 denatured E1 accounted for an increase in fluorescence.
All Science Journal Classification (ASJC) codes
- Analytical Chemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry