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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the membrane part of the enzyme is functionally connected to the active site | Thermus thermophilus | 16020 | - |
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 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 | 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 (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 | 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 | 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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Thermus thermophilus |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 8 | - |
Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Thermus thermophilus | |
heme | the enzyme contains two heme b cofactors, a di-heme | Thermus thermophilus |
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 |