BRENDA - Enzyme Database

Atypical features of Thermus thermophilus succinate:quinone reductase

Kolaj-Robin, O.; Noor, M.R.; OKane, S.R.; Baymann, F.; Soulimane, T.; PLoS ONE 8, e53559 (2013)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.3.5.1
recombinant expression of C-terminally His6-tagged or N-termminally His8-tagged enzyme in Thermus thermophilus under the control of a constitutive promoter
Thermus thermophilus
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.3.5.1
3-nitropropionic acid
-
Thermus thermophilus
1.3.5.1
malonate
-
Thermus thermophilus
1.3.5.1
nonyl-4-hydroxyquinoline-N-oxide
the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties
Thermus thermophilus
1.3.5.1
oxaloacetate
-
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
interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures
Thermus thermophilus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.3.5.1
membrane
-
Thermus thermophilus
16020
-
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.3.5.1
Fe2+
the enzyme contains a [3Fe-4S] center
Thermus thermophilus
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.3.5.1
119800
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration
Thermus thermophilus
1.3.5.1
120000
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer; 3 * 120000, about, wild-type enzyme, SDS-PAGE; 4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
Thermus thermophilus
1.3.5.1
500000
-
wild-type enzyme, consisting of 360 kDa from protein and an unknown contribution of detergent and lipid, native PAGE
Thermus thermophilus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.3.5.1
succinate + menaquinone
Thermus thermophilus
-
fumarate + menaquinol
-
-
?
1.3.5.1
succinate + menaquinone
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
fumarate + menaquinol
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.3.5.1
Thermus thermophilus
-
-
-
1.3.5.1
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.3.5.1
recombinant His6- or His8-tagged enzyme from Thermus thermophilus by nickel affinity chromatography and gel filtration, untagged enzyme by 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
succinate + menaquinone
-
726316
Thermus thermophilus
fumarate + menaquinol
-
-
-
?
1.3.5.1
succinate + menaquinone
-
726316
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + menaquinol
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.3.5.1
monomer
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
Thermus thermophilus
1.3.5.1
tetramer
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
Thermus thermophilus
1.3.5.1
trimer
3 * 120000, about, wild-type enzyme, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.3.5.1
30
-
assay at
Thermus thermophilus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.3.5.1
7.6
-
assay at
Thermus thermophilus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.3.5.1
flavin
covalently-bound flavin cofactor
Thermus thermophilus
1.3.5.1
heme
the enzyme contains two heme b cofactors, a di-heme
Thermus thermophilus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.3.5.1
recombinant expression of C-terminally His6-tagged or N-termminally His8-tagged enzyme in Thermus thermophilus under the control of a constitutive promoter
Thermus thermophilus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.3.5.1
flavin
covalently-bound flavin cofactor
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
malonate
-
Thermus thermophilus
1.3.5.1
nonyl-4-hydroxyquinoline-N-oxide
the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties
Thermus thermophilus
1.3.5.1
oxaloacetate
-
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
interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures
Thermus thermophilus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.3.5.1
membrane
-
Thermus thermophilus
16020
-
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.3.5.1
Fe2+
the enzyme contains a [3Fe-4S] center
Thermus thermophilus
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.3.5.1
119800
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration
Thermus thermophilus
1.3.5.1
120000
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer; 3 * 120000, about, wild-type enzyme, SDS-PAGE; 4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
Thermus thermophilus
1.3.5.1
500000
-
wild-type enzyme, consisting of 360 kDa from protein and an unknown contribution of detergent and lipid, native PAGE
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.3.5.1
succinate + menaquinone
Thermus thermophilus
-
fumarate + menaquinol
-
-
?
1.3.5.1
succinate + menaquinone
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
fumarate + menaquinol
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.3.5.1
recombinant His6- or His8-tagged enzyme from Thermus thermophilus by nickel affinity chromatography and gel filtration, untagged enzyme by 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
succinate + menaquinone
-
726316
Thermus thermophilus
fumarate + menaquinol
-
-
-
?
1.3.5.1
succinate + menaquinone
-
726316
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
fumarate + menaquinol
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.3.5.1
monomer
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer
Thermus thermophilus
1.3.5.1
tetramer
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex
Thermus thermophilus
1.3.5.1
trimer
3 * 120000, about, wild-type enzyme, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.3.5.1
30
-
assay at
Thermus thermophilus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.3.5.1
7.6
-
assay at
Thermus thermophilus
General Information
EC Number
General Information
Commentary
Organism
1.3.5.1
physiological function
succinate:quinone reductase serves as the respiratory complex II
Thermus thermophilus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.3.5.1
physiological function
succinate:quinone reductase serves as the respiratory complex II
Thermus thermophilus