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Literature summary extracted from
- Succinate dehydrogenase and fumrate reductase from Escherichia coli (2002), Biochim. Biophys. Acta, 1553, 140-157.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.5.1 | gene cluster frdABCD encoding 4 subunits, DNA and amino acid sequence analysis, overepression | Escherichia coli |
| 1.3.5.1 | gene cluster sdhCDAB encoding 4 subunits, DNA and amino acid sequence analysis, overepression | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.3.5.1 | PDB code: 1FUM, structure of the QFR monomer, with the covalently bound FAD cofactor, showing the iron-sulfur clusters [4Fe-4S], [3Fe-3S], and [2Fe-2S] and the two menaquinone molecules | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | additional information | His44 mutant contains non-covalently bound FAD and loose the ability to oxidize succinate | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | 2-n-heptyl-4-hydroxyquinoline-N-oxide | - |
Escherichia coli |  |
| 1.3.5.1 | 5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide | i.e., carboxin | Escherichia coli | |
| 1.3.5.1 | Pentachlorophenol | - |
Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.5.1 | additional information | - |
succinate | fumarate reduction. 0.0013 mM, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1 | Escherichia coli | |
| 1.3.5.1 | additional information | - |
fumarate | with menaquinone EC 1.3.5.4, succinate oxidation: 0.003 mM, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.0015 | - |
succinate | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.002 | - |
succinate | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.005 | - |
fumarate | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.0054 | - |
fumarate | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.3.5.1 | membrane | membrane-bound, the catalytic domain is bound to the cytoplasmic membrane by 2 hydrophobic membrane anchor subunits that also form the sites of interaction with quinones | Escherichia coli | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | Iron | iron-sulfur subunit with 3 distinct [4Fe-4S], [3Fe-3S], and [2Fe-2S] clusters, i.e., organized in 2 domains, all participate in electron transfer, overview | Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.5.1 | Escherichia coli | - |
encoded by the sdhCDAB gene clusters | - |
| 1.3.5.1 | Escherichia coli | P00363 | encoded by the frdABCD gene clusters | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.3.5.1 | succinate + a quinone = fumarate + a quinol | can also function as a fumarate reductase | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.5.1 | fumarate + menaquinol | enzyme is expressed under anaerobic conditions, transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1 | Escherichia coli | succinate + menaquinone | - |
r | |
| 1.3.5.1 | succinate + ubiquinone-8 | - |
Escherichia coli | fumarate + ubiquinol-8 | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | More | cf. EC 1.3.5.1, both complexes contain a catalytic domain, composed of a subunit with a covalently bound flavin cofactor, the dicarboxlyate binding site, and an iron-sulfur subunit, which contains three distince iron-sulfur clusters. The catalytic domain is bound to the cytoplasmic membrane by two hydrophobic membrane anchor subunits that also form the sites for interaction with quinones. The catalytic domain is highly conserved and reflect the biochemical and structural similarity of EC 1.3.5.1 (SQR) and 1.3.5.4 (QFR). SQR, in addition to differences in the type of quinones it uses as compared to QFR, is known to contain a single B556 heme moiety, showing to have bis-histidine axial ligation | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | menaquinol-fumarate oxidoreductase | cf. EC 1.3.5.1, succinate-ubiquinone oxidoreductase, structurally and functionally related membrane-bound enzyme complexes | Escherichia coli |
| 1.3.5.1 | QFR | - |
Escherichia coli |
| 1.3.5.1 | SQR | - |
Escherichia coli |
| 1.3.5.1 | succinate-ubiquinone oxidoreductase | cf. EC 1.3.5.4, menaquinol-fumarate oxidoreductase, structurally and functionally related membrane-bound enzyme complexes | Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.3.5.1 | 30 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.5.1 | additional information | - |
succinate | fumarate reduction. 28 s-1, with ubiquinone, reaction of succinate-ubiquinone oxidase EC 1.3.5.1 | Escherichia coli | |
| 1.3.5.1 | additional information | - |
fumarate | with menaquinone EC 1.3.5.4: , succinate oxidation: 3.4 s-1, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 1.7 | - |
fumarate | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 14 | - |
succinate | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 85 | - |
succinate | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 177 | - |
fumarate | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.3.5.1 | 7.8 | - |
assay at | Escherichia coli |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.3.5.1 | additional information | - |
pH profile analysis, both EC 1.3.5.1 and 1.3.5.4 show a similar profile, suggesting that similar amino acid residues may be involved in quinol deprotonation and oxidation in Escherichia coli enzymes | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | FAD | covalently attached to the enzyme to enable succinate oxidation | Escherichia coli | |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.5.1 | additional information | - |
Pentachlorophenol | with menaquinone EC 1.3.5.4, fumarate reduction: 0.013 mM, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | additional information | - |
5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide | with menaquinone EC 1.3.5.4, fumarate reduction: 0.030 mM, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | additional information | - |
Pentachlorophenol | with menaquinone EC 1.3.5.4, succinate oxidation: 0.017 mM, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | additional information | - |
5,6-dihydro-2-methyl-1,4-oxathiin-3-carboxanilide | with menaquinone EC 1.3.5.4, succinate oxidation: 0.035 mM, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.000075 | - |
2-n-heptyl-4-hydroxyquinoline-N-oxide | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.0002 | - |
2-n-heptyl-4-hydroxyquinoline-N-oxide | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.023 | - |
Pentachlorophenol | fumarate reduction, pH 7.8, 30°C | Escherichia coli | |
| 1.3.5.1 | 0.037 | - |
Pentachlorophenol | succinate oxidation, pH 7.8, 30°C | Escherichia coli | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.3.5.1 | Escherichia coli | the QFR complex provides electron transport during anaerobic cell growth conditions. The transcription of the frdABCD operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1, overview | up |
| 1.3.5.1 | Escherichia coli | the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | physiological function | the QFR complex provides electron transport during anaerobic cell growth conditions. The transcription of the frdABCD operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the succinate-ubiquinone oxidase, EC 1.3.5.1, overview | Escherichia coli |
| 1.3.5.1 | physiological function | the SQR complex provides electron transport during aerobic cell growth conditions. The transcription of the sdhCDAB operon responds to environmental as well as internal cell signals to modulate gene expression. The transcription is coupled to that of the menaquinol-fumarate oxidoreductase, EC 1.3.5.4, overview | Escherichia coli |
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