Literature summary extracted from

Condon, C.; Cammack, R.; Patil, D.S.; Owen, P.
The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex (1985), J. Biol. Chem., 260, 9427-9434.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.3.5.1	15000	-	succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE	Escherichia coli
1.3.5.1	26000	-	succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE	Escherichia coli
1.3.5.1	71000	-	succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.3.5.1	Escherichia coli	-	succinate dehydrogenase	-

Subunits

EC Number	Subunits	Comment	Organism
1.3.5.1	tetramer	succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE	Escherichia coli

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.3.5.1	cytochrome b	-	Escherichia coli
1.3.5.1	additional information	measurement of the redox potentials of the sulfur-centers	Escherichia coli
1.3.5.1	additional information	the enzyme contains iron-sulfur centers	Escherichia coli

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Release 2023.1 (January 2023)