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Literature summary for 1.3.5.1 extracted from
- Biochemical and biophysical characterization of succinate: quinone reductase from Thermus thermophilus (2011), Biochim. Biophys. Acta, 1807, 68-79.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-nitropropionic acid | - |
Thermus thermophilus |  |
| diethyl oxaloacetate | - |
Thermus thermophilus | |
| malonate | - |
Thermus thermophilus | |
| nonyl-4-hydroxyquinoline-N-oxide | - |
Thermus thermophilus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetic measurements show that the enzyme displays standard Michaelis-Menten kinetics at a low temperature of 30°C but exhibits deviation from it at a higher temperature of 70°C, the enzyme shows positive cooperativity at higher temperatures | Thermus thermophilus | |
| 0.21 | - |
succinate | pH 7.6, 30°C | Thermus thermophilus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | the membrane part of the enzyme is functionally connected to the active site | Thermus thermophilus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | existence of [2Fe-2S], [4Fe-4S] and [3Fe-4S] iron-sulfur clusters within the purified protein, electron paramagnetic resonance spectroscopy, influence of the substrate on the signal corresponding to the [2Fe-2S] cluster, overview | Thermus thermophilus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 14000 | - |
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE | Thermus thermophilus |
| 15000 | - |
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE | Thermus thermophilus |
| 27000 | - |
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE | Thermus thermophilus |
| 54000 | - |
the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE | Thermus thermophilus |
| 500000 | - |
native PAGE | Thermus thermophilus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermus thermophilus | - |
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase | - |
| Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type enzyme by gel filtration to remove Triton X-100, and anion exchange chromatography, followed by hydroxylapatite chromatography, and again anion exchange chromatography and gel filtration | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | no activity with 1,4-benzoquinone | Thermus thermophilus | ? | - |
? | |
| additional information | no activity with 1,4-benzoquinone | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
| succinate + 1,4-naphthoquinone | with 2,6-dichlorophenolindophenol | Thermus thermophilus | fumarate + 1,4-naphthoquinol | - |
? | |
| succinate + 1,4-naphthoquinone | with 2,6-dichlorophenolindophenol | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | fumarate + 1,4-naphthoquinol | - |
? | |
| succinate + duroquinone | with 2,6-dichlorophenolindophenol | Thermus thermophilus | fumarate + duroquinol | - |
? | |
| succinate + menadione | with 2,6-dichlorophenolindophenol | Thermus thermophilus | fumarate + menadiol | - |
? | |
| succinate + oxidized 2,6-dichlorophenolindophenol | - |
Thermus thermophilus | fumarate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| succinate + oxidized 2,6-dichlorophenolindophenol | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | fumarate + reduced 2,6-dichlorophenolindophenol | - |
? | |
| succinate + oxidized 2,6-dichlorophenolindophenol | - |
Thermus thermophilus | fumarate + reduced 2,6-dichloroindophenol | - |
r | |
| succinate + oxidized 2,6-dichlorophenolindophenol | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | fumarate + reduced 2,6-dichloroindophenol | - |
r | |
| succinate + phenazine methosulfate | with 2,6-dichlorophenolindophenol, best substrate | Thermus thermophilus | fumarate + reduced phenazine methosulfate | - |
? | |
| succinate + phenazine methosulfate | with 2,6-dichlorophenolindophenol, best substrate | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | fumarate + reduced phenazine methosulfate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview | Thermus thermophilus |
| trimer | the enzyme forms a trimer of single subunits consisting of four polypeptides: 1 * 54000, flavoprotein SdhA, + 1 * 27000, iron-sulfur protein SdhB, + 1 * 14000, SdhC, + 1 * 15000, membrane anchor protein SdhD, SDS-PAGE | Thermus thermophilus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DCPIP oxidoreductase | - |
Thermus thermophilus |
| SQR | - |
Thermus thermophilus |
| succinate-2,6-dichlorophenolindophenol oxidoreductase | - |
Thermus thermophilus |
| succinate:quinone reductases | - |
Thermus thermophilus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
- |
Thermus thermophilus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.67 | - |
menadione | with 2,6-dichlorophenolindophenol, pH 7.6, 30°C | Thermus thermophilus | |
| 1.83 | - |
oxidized 2,6-dichlorophenolindophenol | pH 7.6, 30°C | Thermus thermophilus | |
| 2.167 | - |
duroquinone | with 2,6-dichlorophenolindophenol, pH 7.6, 30°C | Thermus thermophilus | |
| 3.67 | - |
1,4-Naphthoquinone | with 2,6-dichlorophenolindophenol, pH 7.6, 30°C | Thermus thermophilus | |
| 8.33 | - |
phenazine methosulfate | with 2,6-dichlorophenolindophenol, pH 7.6, 30°C | Thermus thermophilus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8 | - |
Thermus thermophilus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Thermus thermophilus | |
| heme | the enzyme contains two heme b cofactors, a di-heme | Thermus thermophilus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme as respiratory complex II belongs to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases and quinol:fumarate reductases | Thermus thermophilus |
| additional information | the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview | Thermus thermophilus |
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