PMID:3291870

Citation	Yumoto, N and Tokushige, M (1988) Characterization of multiple fumarase proteins in Escherichia coli. Biochem. Biophys. Res. Commun. 153:1236-43
Abstract	Two different types of fumarase were found in sonic extracts of Escherichia coli; one required Fe-S for the enzyme activity, and the other did not. When the cells were grown without aeration, the Fe-S-independent enzyme occupied over 80% of the overall fumarase activity. Highly purified Fe-S-independent enzyme was suggested to be composed of four subunits (Mr = 48 kDa) by SDS-polyacrylamide gel electrophoresis and gel filtration. Amino acid and N-terminal sequence analyses supported the possibility that the enzyme is a product of fumC gene (FUMC). In aerobically grown cells, however, the content of FUMC was low and the Fe-S-dependent fumarase occupied over 80% of the overall activity. The Fe-S-dependent enzyme appeared to be labile and the activity was rapidly lost during purification. Although the spontaneous inactivation was previously ascribed to thermal lability (S.A. Woods & J.R. Guest (1987) FEMS Microbiol. Lett. 48, 219), the activity could be restored by anaerobic incubation with ferrous ions and SH-compounds.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acids/analysis; Anaerobiosis; Base Sequence; Escherichia coli/enzymology; Ferrous Compounds/metabolism; Fumarate Hydratase/metabolism; Isoenzymes/metabolism; Sulfhydryl Compounds/metabolism
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