Salt-induced changes in the subunit structure of the Bacillus stearothermophilus lipoate acetyltransferase

Yuichi Shigeoka, Tetsuro Fujisawa, Satoshi Teshiba, Hisayoshi Fukumori, Kohji Yamamoto, Yutaka Banno, Yoichi Aso

Research output: Contribution to journalArticlepeer-review


The Bacillus stearothermophilus lipoate acetyltransferase (E2), composed of sixty identical, subunits is the core component of the pyruvate dehydrogenase complex (PDC). E2 polypeptide is composed of LD, PSBD, and CD domains. Most studies had focused on a truncated E2 that is deficient in LD and PSBD, because CD mainly contributes to maintaining the multimeric structure. We examined salt-induced changes in E2 without truncation and constructed reaction models. We speculate that in the presence of KCl, E2 is dissociated into a monomer and then assembled into an aggregative complex (CA) and a quasi-stable complex (CQ). CA was larger than CQ, but smaller than intact E2. CA and CQ were dominant complexes at about neutral pH and at basic pH respectively. PDC, in which PSBD is occupied by other components, and a truncated E2 undergo dissociation only. LD-PSBD region besides CD might then contribute to the partial association of dissociated E2.

Original languageEnglish
Pages (from-to)1637-1644
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Issue number8
Publication statusPublished - 2013

All Science Journal Classification (ASJC) codes

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


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