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Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Caenorhabditis elegans and UniProt Accession Q09545

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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Caenorhabditis elegans
UNIPROT: Q09545
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
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
succinate dehydrogenase
-
complex II
dehydrogenase, succinate
-
-
-
-
Fcc3
-
-
-
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FL cyt
-
-
-
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Flavocytochrome c3
-
-
-
-
FRD
-
-
-
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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
-
-
-
-
Ifc3
-
-
-
-
Iron(III)-induced flavocytochrome C3
-
-
-
-
menaquinol-fumarate oxidoreductase
-
-
-
-
menaquinol:fumarate oxidoreductase
-
-
-
-
succinate dehydrogenase
-
-
succinate dehydrogenase (quinone)
-
-
-
-
succinate dehydrogenase complex
-
-
-
-
succinate oxidoreductase
-
-
-
-
succinate-coenzyme Q reductase
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-
-
-
succinate:quinone oxidoreductase
-
-
succinic acid dehydrogenase
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-
-
-
succinic dehydrogenase
-
-
-
-
succinodehydrogenase
-
-
-
-
succinyl dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
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
-
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 + a quinone
fumarate + a quinol
show the reaction diagram
-
-
-
-
?
additional information
?
-
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 + a quinone
fumarate + a quinol
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe-S-clusters
-
overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the SDH function is regulated through distinct molecular pathways in different species. SDH has evolved to have extra roles in certain microorganisms and immune cells to meet the energy demands of the cells
metabolism
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP
physiological function
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succinate dehydrogenase (SDH), complex II or succinate:quinone oxidoreductase (SQR) is a crucial enzyme involved in both tricarboxylic acid cycle and oxidative phosphorylation, the two primary metabolic pathways for generating ATP. SDH function is tailored in different cell types to meet the energy demands, SDH function is differently regulated in distinct cell types. Enzyme regulation can occur via transcription factors, posttranscriptional regulators and modifiers, e.g. through phosphorylation, deacetylation, succinylation, propionylation, or direct effection, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SDHB_CAEEL
298
0
32891
Swiss-Prot
Mitochondrion (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
classification of subfamilies, comparison of amino acid sequences including EC 1.3.5.1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
posttranslational modifications regulate SDH levels by 4 means: phosphorylation, deacetylation, succinylation and propionylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P211F
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211H
mutant shows significant reduced SDH activity, mutant shows significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate is significantly decreased in mutant compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211L
mutant shows the weakest SDH activity, mutant shows a significant shorter life span compared to wild-type, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, respiration rate in P211L mutant is increased compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
P211N
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211Q
mutant shows significant reduced SDH activity, embryogenesis is impaired in mutant (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type
P211R
mutant shows significant reduced SDH activity, life span of mutant is not reduced compared to wild-type, embryogenesis is impaired in mutant, in P211R mutant are twice as many dead embryos compared to wild-type (dead embryos all arrest before the four-cell stage), mutant shows an increased hypersensitivity to oxidative stress compared to wild-type, mitochondria of mutant generate significantly more superoxide compared to wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA of iron-sulfur subunit
-
cloning of the complete cDNAs for the iron-sulfur protein of complex II
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Amino, H.; Wang, H.; Hirawake, H.; Saruta, F.; Mizuchi, D.; Mineki, R.; Shindo, N.; Murayama, K.; Takamiya, S.; Aoki, T.; Kojima, S.; Kita, K.
Stage-specific isoforms of Ascaris suum complex II: the fumarate reductase of the parasitic adult and the succinate dehydrogenase of free-living larvae share a common iron-sulfur subunit
Mol. Biochem. Parasitol.
106
63-76
2000
Ascaris suum, Caenorhabditis elegans
Manually annotated by BRENDA team
Lemos, R.S.; Fernandes, A.S.; Pereira, M.M.; Gomes, C.M.; Teixeira, M.
Quinol:fumarate oxidoreductases and succinate:quinone oxidoreductases: phylogenetic relationships, metal centers and membrane attachment
Biochim. Biophys. Acta
1553
158-170
2002
Ascaris suum, Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Caenorhabditis elegans, Escherichia coli, facultative anaerobic bacterium, Halobacterium salinarum, Ipomoea batatas, Mammalia, Micrococcus luteus, Mycolicibacterium phlei, Shewanella putrefaciens, Rattus norvegicus, Cereibacter sphaeroides, Rhodospirillum rubrum, Strongyloides ratti, Wolinella succinogenes
Manually annotated by BRENDA team
Huang, J.; Lemire, B.D.
Mutations in the C. elegans succinate dehydrogenase iron-sulfur subunit promote superoxide generation and premature aging
J. Mol. Biol.
387
559-569
2009
Caenorhabditis elegans (Q09545), Caenorhabditis elegans
Manually annotated by BRENDA team
Moosavi, B.; Zhu, X.; Yang, W.; Yang, G.
Genetic, epigenetic and biochemical regulation of succinate dehydrogenase function
Biol. Chem.
401
319-330
2020
Brassica sp., Caenorhabditis elegans, Thermus thermophilus, Staphylococcus aureus, Mycobacterium tuberculosis, Mus musculus, Neisseria meningitidis, Rattus norvegicus, Escherichia coli (P0AC41 AND P07014), Homo sapiens (P31040 AND P21912 AND Q99643 AND O14521), Saccharomyces cerevisiae (Q00711 AND P21801 AND P33421 AND P37298)
Manually annotated by BRENDA team