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Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Sus scrofa

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EC Tree
IUBMB Comments
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
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Word Map
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
succinate dehydrogenase, complex ii, succinic dehydrogenase, mitochondrial complex ii, succinate dehydrogenase complex, mitochondrial succinate dehydrogenase, succinate dehydrogenase subunit b, succinate dehydrogenase b, sdhcdab, succinate-ubiquinone oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
complex II
-
-
-
-
dehydrogenase, succinate
-
-
-
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Fcc3
-
-
-
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FL cyt
-
-
-
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Flavocytochrome c3
-
-
-
-
FRD
-
-
-
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fumarate reductase
-
-
-
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fumarate reductase complex
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-
-
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fumaric hydrogenase
-
-
-
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Ifc3
-
-
-
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Iron(III)-induced flavocytochrome C3
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-
-
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menaquinol-fumarate oxidoreductase
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-
-
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menaquinol:fumarate oxidoreductase
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-
-
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mitochondrial complex II
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mitochondrial succinate:ubiquinone oxidoreductase
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succinate dehydrogenase (quinone)
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-
-
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succinate dehydrogenase complex
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-
-
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succinate oxidoreductase
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-
-
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succinate-coenzyme Q reductase
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-
-
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succinic acid dehydrogenase
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-
-
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succinic dehydrogenase
-
-
-
-
succinodehydrogenase
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-
-
-
succinyl dehydrogenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate:quinone oxidoreductase
A complex generally comprising an FAD-containing component that also binds the carboxylate substrate (A subunit), a component that contains three different iron-sulfur centers [2Fe-2S], [4Fe-4S], and [3Fe-4S] (B subunit), and a hydrophobic membrane-anchor component (C, or C and D subunits) that is also the site of the interaction with quinones. The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of bacteria and archaea, with the hydrophilic domain extending into the mitochondrial matrix and the cytoplasm, respectively. Under aerobic conditions the enzyme catalyses succinate oxidation, a key step in the citric acid (TCA) cycle, transferring the electrons to quinones in the membrane, thus linking the TCA cycle with the aerobic respiratory chain (where it is known as complex II). Under anaerobic conditions the enzyme functions as a fumarate reductase, transferring electrons from the quinol pool to fumarate, and participating in anaerobic respiration with fumarate as the terminal electron acceptor. The enzyme interacts with the quinone produced by the organism, such as ubiquinone, menaquinone, caldariellaquinone, thermoplasmaquinone, rhodoquinone etc. Some of the enzymes contain two heme subunits in their membrane anchor subunit. These enzymes catalyse an electrogenic reaction and are thus classified as EC 7.1.1.12, succinate dehydrogenase (electrogenic, proton-motive force generating).
CAS REGISTRY NUMBER
COMMENTARY hide
9002-02-2
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9028-11-9
-
9076-99-7
cf EC 1.3.1.6
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinate + 2,6-dichlorophenol indophenol
fumarate + reduced 2,6-dichlorophenol indophenol
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
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a key membrane complex in the tricarboxylic acid cycle that catalyzes the oxidation of succinate to fumarate in the mitochondrial matrix as succinate dehydrogenase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ubiquinone
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-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
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noncompetitive inhibition with respect to cytochrome c and 2,6-dichlorophenol indophenol
3-nitropropionate
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-
4,4,4-trifluoro-1-(thiophen-2-yl)butane-1,3-dione
-
-
benodanil
-
noncompetitive
boscalid
-
noncompetitive
carboxin
-
noncompetitive
fenfuram
-
noncompetitive
flutolanil
-
noncompetitive
furametpyr
-
noncompetitive
mepronil
-
noncompetitive
N-[2-(2,4-dichlorophenoxy)phenyl]-3-(difluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
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compound additionally displays good protection effect against Rhizoctonia solani
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
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noncompetitive with respect to 2,6-dichlorophenol indophenol. Compound additionally displays good protection effect against Rhizoctonia solani
oxycarboxin
-
noncompetitive
penthiopyrad
thifluzamide
-
noncompetitive
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000034
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
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pH not specified in the publication, temperature not specified in the publication
0.0132
benodanil
-
pH 7.4,23°C
0.0092
boscalid
-
pH 7.4,23°C
0.0046
carboxin
-
pH 7.4,23°C
0.1084
fenfuram
-
pH 7.4,23°C
0.0289
flutolanil
-
pH 7.4,23°C
0.0293
furametpyr
-
pH 7.4,23°C
0.0318
mepronil
-
pH 7.4,23°C
0.000081
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
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pH not specified in the publication, temperature not specified in the publication
0.081
oxycarboxin
-
pH 7.4,23°C
0.00033 - 0.0039
penthiopyrad
0.0002
thifluzamide
-
pH 7.4,23°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004
3-(difluoromethyl)-1-methyl-N-(1-[(3,5-dimethylphenyl)methyl]indol-7-yl)-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.0128
benodanil
Sus scrofa
-
pH 7.4,23°C
0.0083
boscalid
Sus scrofa
-
pH 7.4,23°C
0.0043
carboxin
Sus scrofa
-
pH 7.4,23°C
0.1233
fenfuram
Sus scrofa
-
pH 7.4,23°C
0.0289
flutolanil
Sus scrofa
-
pH 7.4,23°C
0.0273
furametpyr
Sus scrofa
-
pH 7.4,23°C
0.0304
mepronil
Sus scrofa
-
pH 7.4,23°C
0.0004
N-[2-(2,4-dichlorophenoxy)phenyl]-3-(difluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.000062
N-[2-(2-chloro-4-trifluoromethylphenoxy)phenyl]-3-(2-fluoromethyl)-1-methyl-1H-pyrazole-4-carboxamide
Sus scrofa
-
pH not specified in the publication, temperature not specified in the publication
0.0856
oxycarboxin
Sus scrofa
-
pH 7.4,23°C
0.00053 - 0.0013
penthiopyrad
0.00017
thifluzamide
Sus scrofa
-
pH 7.4,23°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SDHA_PIG
664
0
72832
Swiss-Prot
Mitochondrion (Reliability: 1)
SDHB_PIG
280
0
31586
Swiss-Prot
Mitochondrion (Reliability: 3)
A0A4X1W8G3_PIG
280
0
31585
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D0MRA7_PIG
225
0
25641
TrEMBL
other Location (Reliability: 4)
A0A4X1TFA7_PIG
635
0
69820
TrEMBL
other Location (Reliability: 2)
A0A5G2R6Z8_PIG
583
0
63624
TrEMBL
Mitochondrion (Reliability: 1)
I3LDC1_PIG
280
0
31585
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D0JA85_PIG
562
0
61258
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D0YW23_PIG
555
0
60521
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D1U304_PIG
616
0
67424
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D1MW88_PIG
583
0
63624
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0W5C8_PIG
264
0
29724
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D0TZY6_PIG
649
0
71195
TrEMBL
Mitochondrion (Reliability: 5)
A0A4X1TJ75_PIG
533
0
58274
TrEMBL
other Location (Reliability: 1)
A0A4X1TJ70_PIG
566
0
62074
TrEMBL
other Location (Reliability: 1)
A0A8D1KD80_PIG
658
0
72128
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D2ACY1_PIG
665
0
72960
TrEMBL
Mitochondrion (Reliability: 1)
A0A5G2QMG3_PIG
616
0
67424
TrEMBL
Mitochondrion (Reliability: 1)
A0A4X1TJN2_PIG
614
0
67481
TrEMBL
other Location (Reliability: 1)
A0A8D0JMP8_PIG
595
0
65058
TrEMBL
Mitochondrion (Reliability: 4)
A0A5G2Q7D7_PIG
649
0
71195
TrEMBL
Mitochondrion (Reliability: 5)
A0A8D0W630_PIG
328
0
36287
TrEMBL
Mitochondrion (Reliability: 3)
A0A8D1ULI3_PIG
280
0
31611
TrEMBL
Mitochondrion (Reliability: 4)
A0A8A0RRK7_PIG
208
0
23665
TrEMBL
other Location (Reliability: 2)
A0A480LCX7_PIG
664
0
72832
TrEMBL
Mitochondrion (Reliability: 1)
A0A5G2R1P2_PIG
328
0
36301
TrEMBL
Mitochondrion (Reliability: 3)
A0A480U0T9_PIG
645
0
70085
TrEMBL
Mitochondrion (Reliability: 1)
A0A8D0YUF7_PIG
588
0
64320
TrEMBL
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
complex II is comprised of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two transmembrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone
dimer
-
biosynthesis and processing
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structure of complex II from porcine heart at 2.4 A resolution and its complex structure with inhibitors 3-nitropropionate and 2-thenoyltrifluoroacetone at 3.5 A resolution
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molecular docking, molecular dynamics simulation, and molecular mechanics/Poisson-Boltzmann surface area calculations for complexes with carboxamide inhibitors. The acid moiety of carboxamide fungicides inserts into the ubiquinone binding site of SQR, forming van der Waals interactions with subunit C residues R46, S42, and subunit B residues I218, and P169, while the amine moiety extends to the mouth of the Q-site, forming van der Waals interactions with subunit C residues W35, I43, and I30. The carbonyl oxygen atom of the carboxamide forms hydrogen bonds with subunit B W173 and subunit DY91
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partially purified enzyme, crystal growth in ammonium sulfate preparation precipitate, X-ray diffraction structure determination and analysis at 2.4 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme complex from heart partially by ammonium sulfate fractionation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clarkson, G.H.D.; King, T.E.; Lindsay, J.G.
Biosynthesis and processing of the large and small subunits of succinate dehydrogenase in cultured mammalian cells
Biochem. J.
244
15-20
1987
Mammalia, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Sun, F.; Huo, X.; Zhai, Y.; Wang, A.; Xu, J.; Su, D.; Bartlam, M.; Rao, Z.
Crystal structure of mitochondrial respiratory membrane protein complex II
Cell
121
1043-1057
2005
Sus scrofa
Manually annotated by BRENDA team
Huo, X.; Su, D.; Wang, A.; Zhai, Y.; Xu, J.; Li, X.; Bartlam, M.; Sun, F.; Rao, Z.
Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart
FEBS J.
274
1524-1529
2007
Sus scrofa
Manually annotated by BRENDA team
Zhu, X.L.; Xiong, L.; Li, H.; Song, X.Y.; Liu, J.J.; Yang, G.F.
Computational and experimental insight into the molecular mechanism of carboxamide inhibitors of succinate-ubquinone oxidoreductase
ChemMedChem
9
1512-1521
2014
Sus scrofa
Manually annotated by BRENDA team
Xiong, L.; Zhu, X.L.; Gao, H.W.; Fu, Y.; Hu, S.Q.; Jiang, L.N.; Yang, W.C.; Yang, G.F.
Discovery of potent succinate-ubiquinone oxidoreductase inhibitors via pharmacophore-linked fragment virtual screening approach
J. Agric. Food Chem.
64
4830-4837
2016
Rhizoctonia solani, Sus scrofa
Manually annotated by BRENDA team
Xiong, L.; Li, H.; Jiang, L.N.; Ge, J.M.; Yang, W.C.; Zhu, X.L.; Yang, G.F.
Structure-based discovery of potential fungicides as succinate ubiquinone oxidoreductase inhibitors
J. Agric. Food Chem.
65
1021-1029
2017
Sus scrofa
Manually annotated by BRENDA team