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MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases
Takefumi Shimoyama1, Eranna Rajashekhara, Daijiro Ohmori
1Marine Biotechnology Institute, Heita, Kamaishi, Iwate, Japan. takefumi.shimoyama@mbio.jp
Abstract:
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 degrees 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.
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