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Information on EC 1.3.5.1 - succinate dehydrogenase

for references in articles please use BRENDA:EC1.3.5.1
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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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This record set is specific for:
UNIPROT: Q99643
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Word Map
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 of the respiratory chain
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dehydrogenase/complex II
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complex II
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dehydrogenase, succinate
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Fcc3
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FL cyt
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-
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Flavocytochrome c3
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-
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FRD
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-
-
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fumarate reductase
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-
-
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fumarate reductase complex
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-
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fumaric hydrogenase
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-
-
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Ifc3
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-
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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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succinate dehydrogenase (quinone)
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succinate dehydrogenase complex
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succinate oxidoreductase
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succinate-coenzyme Q reductase
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succinic acid dehydrogenase
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succinic dehydrogenase
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succinodehydrogenase
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-
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succinyl dehydrogenase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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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
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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 + ubiquinone
fumarate + ubiquinol
show the reaction diagram
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-
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?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene SDHC; subunit C encoding gene SDHC
UniProt
Manually annotated by BRENDA team
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?
C560_HUMAN
169
0
18610
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit C encoding gene SDHC, DNA and amino acid sequence determination, genotyping, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bonache, S.; Martinez, J.; Fernandez, M.; Bassas, L.; Larriba, S.
Single nucleotide polymorphisms in succinate dehydrogenase subunits and citrate synthase genes: association results for impaired spermatogenesis
Int. J. Androl.
30
144-152
2007
Homo sapiens, Homo sapiens (P21912), Homo sapiens (Q99643)
Manually annotated by BRENDA team