Thermal Disassembly of Pyruvate Dehydrogenase Multienzyme Complex from Bacillus Stearothermophilus

Yasuaki Hiromasa, Yoichi Aso, Shoji Yamashita

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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
Volume58
Issue number10
DOIs
Publication statusPublished - 1994

Fingerprint

Naphthalenesulfonates
Multienzyme Complexes
Pyruvate Dehydrogenase Complex
Geobacillus stearothermophilus
Bacilli
Pyruvic Acid
Oxidoreductases
Dihydrolipoyllysine-Residue Acetyltransferase
Hot Temperature
Fluorescence
Pyruvate Decarboxylase
Dihydrolipoamide Dehydrogenase
Denaturation
Enzymes

All Science Journal Classification (ASJC) codes

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

Cite this

Thermal Disassembly of Pyruvate Dehydrogenase Multienzyme Complex from Bacillus Stearothermophilus. / Hiromasa, Yasuaki; Aso, Yoichi; Yamashita, Shoji.

In: Bioscience, Biotechnology, and Biochemistry, Vol. 58, No. 10, 1994, p. 1904-1905.

Research output: Contribution to journalArticle

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