Thermal Disassembly of Pyruvate Dehydrogenase Multienzyme Complex from Bacillus Stearothermophilus

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1904-1905
Number of pages2
JournalBioscience, biotechnology, and biochemistry
Issue number10
Publication statusPublished - 1994

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


Dive into the research topics of 'Thermal Disassembly of Pyruvate Dehydrogenase Multienzyme Complex from Bacillus Stearothermophilus'. Together they form a unique fingerprint.

Cite this