MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases

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

doi:10.1111/j.1574-6968.2007.00665.x

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 journal › Article › peer-review

13 Citations (Scopus)

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°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 language	English
Pages (from-to)	207-213
Number of pages	7
Journal	FEMS Microbiology Letters
Volume	270
Issue number	2
DOIs	https://doi.org/10.1111/j.1574-6968.2007.00665.x
Publication status	Published - 2007 May
Externally published	Yes

Keywords

Fumarase
Fumarate
Iron-sulfur cluster
Methane fermentation
Propionate
Syntrophic bacteria

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

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10.1111/j.1574-6968.2007.00665.x

Cite this

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title = "MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases",

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°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.",

keywords = "Fumarase, Fumarate, Iron-sulfur cluster, Methane fermentation, Propionate, Syntrophic bacteria",

author = "Takefumi Shimoyama and Eranna Rajashekhara and Daijiro Ohmori and Tomoyuki Kosaka and Kazuya Watanabe",

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T1 - MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases

AU - Shimoyama, Takefumi

AU - Rajashekhara, Eranna

AU - Ohmori, Daijiro

AU - Kosaka, Tomoyuki

AU - Watanabe, Kazuya

PY - 2007/5

Y1 - 2007/5

N2 - 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.

AB - 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.

KW - Fumarase

KW - Fumarate

KW - Iron-sulfur cluster

KW - Methane fermentation

KW - Propionate

KW - Syntrophic bacteria

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MmcBC in Pelotomaculum thermopropionicum represents a novel group of prokaryotic fumarases

Abstract

Keywords

ASJC Scopus subject areas

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