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Literature summary extracted from
- Succinate:quinone oxidoreductases: new insights from x-ray crystal structures (2000), Biochim. Biophys. Acta, 1459, 422-431.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.3.5.1 | structure of subunits, binding sites, structure of complex II, pathway of electron transfer | Bacillus subtilis |
| 1.3.5.1 | structure of subunits, binding sites, structure of complex II, pathway of electron transfer | Escherichia coli |
| 1.3.5.1 | structure of subunits, binding sites, structure of complex II, pathway of electron transfer | Wolinella succinogenes |
| 1.3.5.1 | the structure of the enzyme is determined at 2.2 A resolution by X-ray crystallography | Wolinella succinogenes |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.3.5.1 | membrane | - |
Wolinella succinogenes | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | Iron | attached to menaquinol-oxidising subunit C on the cytoplasmic side of the membrane is subunit B, containing the [3Fe-4S], [4Fe-4S], and [2Fe-2S] iron-sulphur centres (in the order of increasing distance from menaquinol-oxidising subunit C) | Wolinella succinogenes |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.5.1 | succinate + a menaquinone | Wolinella succinogenes | the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate | fumarate + a menaquinol | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.5.1 | Bacillus subtilis | - |
- |
- |
| 1.3.5.1 | Escherichia coli | - |
- |
- |
| 1.3.5.1 | Wolinella succinogenes | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.5.1 | additional information | pathway of electron transfer in complex II | Bacillus subtilis | ? | - |
? | |
| 1.3.5.1 | additional information | pathway of electron transfer in complex II | Escherichia coli | ? | - |
? | |
| 1.3.5.1 | additional information | pathway of electron transfer in complex II | Wolinella succinogenes | ? | - |
? | |
| 1.3.5.1 | succinate + a menaquinone | - |
Wolinella succinogenes | fumarate + a menaquinol | - |
? | |
| 1.3.5.1 | succinate + a menaquinone | the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate | Wolinella succinogenes | fumarate + a menaquinol | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | QFR | - |
Escherichia coli |
| 1.3.5.1 | QFR | - |
Wolinella succinogenes |
| 1.3.5.1 | SQR | - |
Bacillus subtilis |
| 1.3.5.1 | SQR | - |
Escherichia coli |
| 1.3.5.1 | succinate:menaquinone reductase | - |
Wolinella succinogenes |
| 1.3.5.1 | succinate:MK reductase | - |
Wolinella succinogenes |
| 1.3.5.1 | succinate:quinone oxidoreductase | ambiguous | Bacillus subtilis |
| 1.3.5.1 | succinate:quinone oxidoreductase | ambiguous | Escherichia coli |
| 1.3.5.1 | succinate:quinone oxidoreductase | ambiguous | Wolinella succinogenes |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | FAD | subunit A comprises a large FAD-binding domain | Wolinella succinogenes | |
| 1.3.5.1 | heme b | the enzyme contains one hydrophobic subunit (C) with two haem b groups | Bacillus subtilis | |
| 1.3.5.1 | heme b | the enzyme contains one hydrophobic subunit (menaquinol-oxidising subunit C) with two haem b groups. The binding of the two heme molecules is described. The close proximity between the two hemes offers a straightforward possibility for transmembrane electron transfer | Wolinella succinogenes | |
| 1.3.5.1 | additional information | two hydrophobic subunits (C and D) which bind either no haem b group | Escherichia coli | |
| 1.3.5.1 | additional information | two hydrophobic subunits (C and D) which bind either one haem b group | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | physiological function | is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate | Escherichia coli |
| 1.3.5.1 | physiological function | the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain | Bacillus subtilis |
| 1.3.5.1 | physiological function | the enzyme is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain | Escherichia coli |
| 1.3.5.1 | physiological function | the enzyme is involved in anaerobic respiration with fumarate as the terminal electron acceptor, and is part of an electron transport chain catalysing the oxidation of various donor substrates by fumarate | Wolinella succinogenes |
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