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1.3.5.1: succinate dehydrogenase

This is an abbreviated version!
For detailed information about succinate dehydrogenase, go to the full flat file.

Word Map on EC 1.3.5.1

Reaction

succinate
+
a quinone
=
fumarate
+
a quinol

Synonyms

8-methylmenaquinol:fumarate reductase, AaSdhB, bacterial succinate:quinone oxidoreductase flavoprotein, complex II, Complex II homolog, complex II of the respiratory chain, complex II succinate:ubiquinone oxidoreductase, DCPIP oxidoreductase, dehydrogenase, succinate, dehydrogenase/complex II, EC 1.3.5.4, EC 1.3.99.1, Fcc3, fdrB, FL cyt, Flavocytochrome c3, FRD, FrdA, FRdABCD, FrdC, FRdCAB, FrdD, fumarate reductase, fumarate reductase complex, fumaric hydrogenase, Ifc3, Iron(III)-induced flavocytochrome C3, iron-sulfur subunit of succinate dehydrogenase, menaquinol-1 fumarate reductase, menaquinol-fumarate oxidoreductase, menaquinol:fumarate oxidoreductase, methylmenaquinol:fumarate reductase, MFR, MFR complex, MfrA, MfrB, mitochondrial complex II, mitochondrial succinate dehydrogenase, mitochondrial succinate:ubiquinone oxidoreductase, More, mQFR, MSMEG_0416, MSMEG_0417, MSMEG_0418, MSMEG_0419, MSMEG_0420, MSMEG_1669, MSMEG_1670, MSMEG_1671, MSMEG_1672, non-classical succinate:quinone reductase, QFR, quinol-fumarate reductase, quinol:fumarate reductase, SDG, SDG-1, SDG-2, SDH, SDH1, SDH2, SDH2-1, SDH2-2, SDH3, SDH4, SdhA, sdhABE, SDHB, SdhC, sdhCAB, SdhCDAB, SdhD, SDISP, SQR, succinate dehydrogenase, succinate dehydrogenase (caldariellaquinone), succinate dehydrogenase (quinone), succinate dehydrogenase B, succinate dehydrogenase complex, succinate dehydrogenase flavoprotein subunit Sdh1p, succinate dehydrogenase iron-sulfur protein, succinate dehydrogenase iron-sulphur protein, succinate dehydrogenase subunit B, succinate oxidoreductase, succinate-2,6-dichlorophenolindophenol oxidoreductase, succinate-coenzyme Q reductase, succinate-quinone oxidoreductase, succinate-quinone reductase, succinate-ubiquinone oxidoreductase, succinate:caldariellaquinone oxidoreductase, succinate:menaquinone 7-reductase, succinate:menaquinone oxidoreductase, succinate:menaquinone reductase, succinate:MK reductase, succinate:quinone oxidoreductase, succinate:quinone reductase, succinate:quinone reductases, succinate:ubiquinone oxidoreductase, succinate:ubiquinone reductase, succinic acid dehydrogenase, succinic dehydrogenase, succinodehydrogenase, succinyl dehydrogenase, Tneu_0423

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.5 With a quinone or related compound as acceptor
                1.3.5.1 succinate dehydrogenase

Molecular Weight

Molecular Weight on EC 1.3.5.1 - succinate dehydrogenase

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
11000
-
1 * 66000 + 1 * 27000 + 1 * 12000 + 1 * 11000, SDS-PAGE
110000
-
PAGE
110000 - 114000
-
excluding cytochrome b, calculation from FAD-content and subunit composition
11100
118000
-
calculation from subunit composition
119800
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration
12000
120000
12800
x * 66000 (subunit a) + x * 31000 (subunit b) + x * 28000 (subunit c) + x * 12800 (subunit d), the four subunits are present in an equimolar stoichiometry, SDS-PAGE
13000
135000
-
high resolution clear-native electrophoresis
13900
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
14000
14080
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
14300
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
147000
-
calculation from Stokes radius and sedimentation coefficient
15000
150000
-
blue native gel electrophoresis
15300
160000 - 167000
-
including cytochrome b, calculation from FAD-content and subunit composition
16638
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
16675
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
17000
-
1 * 72000 (flavoprotein) + 1* 30000, and 1 * 15000 + 1 * 17000 as membrane anchor (at least one of the latter a cytochrome b-protein), precipitation of protein with specific antibody and SDS-PAGE
170000
-
sedimentation equilibrium centrifugation of preparation containing Triton X-100
18000
-
1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE
180000
-
dimeric form, gel filtration
200000
23000
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
25000
26000
260000
-
Blue-native PAGE
27000
27097
28000
28064
28400
29000
-
3 * 29000 + 3 * 67000 + 3 * 23000, homotrimeric complex of the protomer composed of three different subunits (29000 Da, 67000 Da and 23000 Da), SDS-PAGE
29600
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
30000
30229
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
31000
32000
32205
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
33000
35000
-
iron-sulphur subunit
36471
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
37000
-
x * 66000 + x * 37000 + x * 33000 + x * 12000, presence of very strong protein protein interactions among the 66000 Da, the 37000 Da and the 12000 Da subunit, and of weaker interactions between the 33000 Da subunit and the rest of the subunits, SDS-PAGE
410000
500000
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
60000
-
1 * 60000 + 1* 25000, SDS-PAGE
62000
-
? * 62000 + ? * 26000
63000
x * 63000, SDS-PAGE
63075
x * 63075 (flavoprotein subunit SdhA) + x * 36471 (iron-sulfur protein SdhB) + x * 32205 (subunit SdhC) + x * 14080 (subunit SdhD). Subunit SdhA and SdhB show characteristic sequence similarities to the succinate dehydrogenases and fumarate reductases of other organisms, while the SdhC and SdhD subunits, thought to form the membrane-anchoring domain, lack typical transmembrane alpha-helical regions present in all other succinate:quinone reductases and quinol:fumarate reductases
64000
-
1 * 64000 + 1 * 28000 + 1+ 14000 + 1 * 13000, SDS-PAGE
65000
65600
-
1 * 65600 + 1 * 29600 + 1 * 14300 + 1 * 13900
66000
67000
68000
69000
-
fumarate reductase, membrane-extrinsic domain: 1 * 69000 + 1 * 27000, membrane-intrinsic domain: 1 * 15000 + 1 * 13000 containing cytochrome b, necessary for converting succinate dehydrogenase EC 1.3.99.1 into succinate-ubiquinone oxidoreductase
7000
-
1 * 7000 + 1* 27000, SDS-PAGE
70000
70185
-
1 * 70185, + 1 * 30229, + 1 * 16675, + 1 * 16638, subunits Sdh1, Sdh2, Sdh3 and Sdh4
71000
-
succinate dehydrogenase, 1 * 71000 + 1 * 26000 + 1 + 17000 + 1 * 15000, immunoprecipitation followed by SDS-PAGE
72000
73000
-
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer
73234
79000
90000 - 100000
97000 - 105000