BRENDA - Enzyme Database

Biochemical and biophysical characterization of succinate: quinone reductase from Thermus thermophilus

Kolaj-Robin, O.; OKane, S.R.; Nitschke, W.; Leger, C.; Baymann, F.; Soulimane, T.; Biochim. Biophys. Acta 1807, 68-79 (2011)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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
Commentary
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
Commentary
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]
Commentary
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.3.5.1
additional information
no activity with 1,4-benzoquinone
724421
Thermus thermophilus
?
-
-
-
-
1.3.5.1
additional information
no activity with 1,4-benzoquinone
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
?
-
-
-
-
1.3.5.1
succinate + 1,4-naphthoquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + 1,4-naphthoquinol
-
-
-
?
1.3.5.1
succinate + 1,4-naphthoquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + 1,4-naphthoquinol
-
-
-
?
1.3.5.1
succinate + duroquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + duroquinol
-
-
-
?
1.3.5.1
succinate + duroquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + duroquinol
-
-
-
?
1.3.5.1
succinate + menadione
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + menadiol
-
-
-
?
1.3.5.1
succinate + oxidized 2,6-dichlorophenolindophenol
-
724421
Thermus thermophilus
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.3.5.1
succinate + oxidized 2,6-dichlorophenolindophenol
-
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.3.5.1
succinate + phenazine methosulfate
with 2,6-dichlorophenolindophenol, best substrate
724421
Thermus thermophilus
fumarate + reduced phenazine methosulfate
-
-
-
?
1.3.5.1
succinate + phenazine methosulfate
with 2,6-dichlorophenolindophenol, best substrate
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + reduced phenazine methosulfate
-
-
-
?
Subunits
EC Number
Subunits
Commentary
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
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
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
Commentary
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
-
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
Commentary
Organism
1.3.5.1
7
8
-
Thermus thermophilus
Cofactor
EC Number
Cofactor
Commentary
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
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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 (protein specific)
EC Number
Localization
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
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
Purification (Commentary) (protein specific)
EC Number
Commentary
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) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.3.5.1
additional information
no activity with 1,4-benzoquinone
724421
Thermus thermophilus
?
-
-
-
-
1.3.5.1
additional information
no activity with 1,4-benzoquinone
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
?
-
-
-
-
1.3.5.1
succinate + 1,4-naphthoquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + 1,4-naphthoquinol
-
-
-
?
1.3.5.1
succinate + 1,4-naphthoquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + 1,4-naphthoquinol
-
-
-
?
1.3.5.1
succinate + duroquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + duroquinol
-
-
-
?
1.3.5.1
succinate + duroquinone
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + duroquinol
-
-
-
?
1.3.5.1
succinate + menadione
with 2,6-dichlorophenolindophenol
724421
Thermus thermophilus
fumarate + menadiol
-
-
-
?
1.3.5.1
succinate + oxidized 2,6-dichlorophenolindophenol
-
724421
Thermus thermophilus
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.3.5.1
succinate + oxidized 2,6-dichlorophenolindophenol
-
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
1.3.5.1
succinate + phenazine methosulfate
with 2,6-dichlorophenolindophenol, best substrate
724421
Thermus thermophilus
fumarate + reduced phenazine methosulfate
-
-
-
?
1.3.5.1
succinate + phenazine methosulfate
with 2,6-dichlorophenolindophenol, best substrate
724421
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + reduced phenazine methosulfate
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
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
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.3.5.1
70
-
-
Thermus thermophilus
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
-
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 (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.3.5.1
7
8
-
Thermus thermophilus
General Information
EC Number
General Information
Commentary
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
General Information (protein specific)
EC Number
General Information
Commentary
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