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Literature summary extracted from

  • Kolaj-Robin, O.; OKane, S.R.; Nitschke, W.; Leger, C.; Baymann, F.; Soulimane, T.
    Biochemical and biophysical characterization of succinate: quinone reductase from Thermus thermophilus (2011), Biochim. Biophys. Acta, 1807, 68-79.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 3-nitropropionic acid
-
Thermus thermophilus
1.3.5.1 diethyl oxaloacetate
-
Thermus thermophilus
1.3.5.1 malonate
-
Thermus thermophilus
1.3.5.1 nonyl-4-hydroxyquinoline-N-oxide
-
Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 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
1.3.5.1 0.21
-
succinate pH 7.6, 30°C Thermus thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 membrane the membrane part of the enzyme is functionally connected to the active site Thermus thermophilus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.5.1 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
1.3.5.1 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
1.3.5.1 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
1.3.5.1 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
1.3.5.1 500000
-
native PAGE Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Thermus thermophilus
-
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase
-
1.3.5.1 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
gene products of sdhDCAB operon as genuine subunits of succinate:quinone reductase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 additional information no activity with 1,4-benzoquinone Thermus thermophilus ?
-
?
1.3.5.1 additional information no activity with 1,4-benzoquinone Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
?
1.3.5.1 succinate + 1,4-naphthoquinone with 2,6-dichlorophenolindophenol Thermus thermophilus fumarate + 1,4-naphthoquinol
-
?
1.3.5.1 succinate + 1,4-naphthoquinone with 2,6-dichlorophenolindophenol Thermus thermophilus HB8 / ATCC 27634 / DSM 579 fumarate + 1,4-naphthoquinol
-
?
1.3.5.1 succinate + duroquinone with 2,6-dichlorophenolindophenol Thermus thermophilus fumarate + duroquinol
-
?
1.3.5.1 succinate + menadione with 2,6-dichlorophenolindophenol Thermus thermophilus fumarate + menadiol
-
?
1.3.5.1 succinate + oxidized 2,6-dichlorophenolindophenol
-
Thermus thermophilus fumarate + reduced 2,6-dichlorophenolindophenol
-
?
1.3.5.1 succinate + oxidized 2,6-dichlorophenolindophenol
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 fumarate + reduced 2,6-dichlorophenolindophenol
-
?
1.3.5.1 succinate + oxidized 2,6-dichlorophenolindophenol
-
Thermus thermophilus fumarate + reduced 2,6-dichloroindophenol
-
r
1.3.5.1 succinate + oxidized 2,6-dichlorophenolindophenol
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 fumarate + reduced 2,6-dichloroindophenol
-
r
1.3.5.1 succinate + phenazine methosulfate with 2,6-dichlorophenolindophenol, best substrate Thermus thermophilus fumarate + reduced phenazine methosulfate
-
?
1.3.5.1 succinate + phenazine methosulfate with 2,6-dichlorophenolindophenol, best substrate Thermus thermophilus HB8 / ATCC 27634 / DSM 579 fumarate + reduced phenazine methosulfate
-
?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 More circular dichroism and blue-native polyacrylamide gel electrophoresis reveal that the enzyme forms a trimer with a predominantly helical fold, overview Thermus thermophilus
1.3.5.1 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

EC Number Synonyms Comment Organism
1.3.5.1 DCPIP oxidoreductase
-
Thermus thermophilus
1.3.5.1 SQR
-
Thermus thermophilus
1.3.5.1 succinate-2,6-dichlorophenolindophenol oxidoreductase
-
Thermus thermophilus
1.3.5.1 succinate:quinone reductases
-
Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 70
-
-
Thermus thermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.5.1 1.67
-
menadione with 2,6-dichlorophenolindophenol, pH 7.6, 30°C Thermus thermophilus
1.3.5.1 1.83
-
oxidized 2,6-dichlorophenolindophenol pH 7.6, 30°C Thermus thermophilus
1.3.5.1 2.167
-
duroquinone with 2,6-dichlorophenolindophenol, pH 7.6, 30°C Thermus thermophilus
1.3.5.1 3.67
-
1,4-Naphthoquinone with 2,6-dichlorophenolindophenol, pH 7.6, 30°C Thermus thermophilus
1.3.5.1 8.33
-
phenazine methosulfate with 2,6-dichlorophenolindophenol, pH 7.6, 30°C Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.5.1 7 8
-
Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 FAD
-
Thermus thermophilus
1.3.5.1 heme the enzyme contains two heme b cofactors, a di-heme Thermus thermophilus

General Information

EC Number General Information Comment Organism
1.3.5.1 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
1.3.5.1 additional information the membrane part of the enzyme is functionally connected to the active site, structure-function relationship, overview Thermus thermophilus