MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases

Takefumi Shimoyama, Eranna Rajashekhara, Daijiro Ohmori, Tomoyuki Kosaka, Kazuya Watanabe

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


The overall amino-acid sequence of MmcBC in Pelotomaculum thermopropionicum was substantially homologous (33%) to fumarase A in Escherichia coli, although its possible subunit structure was different from known fumarases and it lacked the fumarate-lyase signature sequence. Here, MmcBC in E. coli is expressed and characterized. The purified enzyme catalyzed reversible conversion of fumarate to l-malate at an optimum temperature of 70°C. Its molecular size was 64.2 kDa, indicating that it consisted of one MmcB and one MmcC. EPR spectra revealed that it had an oxygen-sensitive [4Fe-4S] cluster. We propose that MmcBC represents a novel group of prokaryotic fumarases.

Original languageEnglish
Pages (from-to)207-213
Number of pages7
JournalFEMS Microbiology Letters
Issue number2
Publication statusPublished - 2007 May
Externally publishedYes


  • Fumarase
  • Fumarate
  • Iron-sulfur cluster
  • Methane fermentation
  • Propionate
  • Syntrophic bacteria

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


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