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Information on EC 1.3.5.1 - succinate dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P21912

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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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Homo sapiens
UNIPROT: P21912
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
-
dehydrogenase/complex II
-
complex II
complex II of the respiratory chain
-
complex II succinate:ubiquinone oxidoreductase
-
-
dehydrogenase, succinate
-
-
-
-
dehydrogenase/complex II
-
Fcc3
-
-
-
-
FL cyt
-
-
-
-
Flavocytochrome c3
-
-
-
-
FRD
-
-
-
-
fumarate reductase
-
-
-
-
fumarate reductase complex
-
-
-
-
fumaric hydrogenase
-
-
-
-
Ifc3
-
-
-
-
Iron(III)-induced flavocytochrome C3
-
-
-
-
menaquinol-fumarate oxidoreductase
-
-
-
-
menaquinol:fumarate oxidoreductase
-
-
-
-
mitochondrial complex II
-
-
succinate dehydrogenase
succinate dehydrogenase (quinone)
-
-
-
-
succinate dehydrogenase B
-
-
succinate dehydrogenase complex
-
-
-
-
succinate dehydrogenase subunit B
-
-
succinate oxidoreductase
-
-
-
-
succinate-coenzyme Q reductase
-
-
-
-
succinate:quinone oxidoreductase
P31040; P21912; Q99643; O14521
-
succinic acid dehydrogenase
-
-
-
-
succinic dehydrogenase
-
-
-
-
succinodehydrogenase
-
-
-
-
succinyl dehydrogenase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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 + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + a quinone
fumarate + a quinol
show the reaction diagram
P31040; P21912; Q99643; O14521
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
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 + ubiquinone
fumarate + ubiquinol
show the reaction diagram
-
-
-
?
succinate + a quinone
fumarate + a quinol
show the reaction diagram
P31040; P21912; Q99643; O14521
-
-
-
?
succinate + FAD
fumarate + FADH2
show the reaction diagram
-
-
-
-
?
succinate + ubiquinone
fumarate + ubiquinol
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe-S center
-
the Fe-S centers in Sdh2 consist of a 2Fe-2S center proximal to the FAD site, an adjacent 4Fe-4S center followed by a 3Fe-4S center
Fe-S cluster
P31040; P21912; Q99643; O14521
SDHB is an iron-sulfur cluster protein containing three Fe-S clusters
heme
P31040; P21912; Q99643; O14521
SDHC and SDHD subunits are alpha-helical transmembrane proteins which ligate a single heme between them
heme b
-
-
ubiquinone
additional information
-
the enzyme contains iron-sulfur centers
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Thenoyltrifluoroacetone
-
-
atpenin A5
-
0.0000042 mM, 50% inhibition
malonate
-
0.18 mM, 50% inhibition
oxaloacetate
P31040; P21912; Q99643; O14521
the interaction between SDH and oxaloacetate renders the enzyme inactive, while the interaction between the activator and enzyme prevent such interaction with oxaloacetate
thenoyltrifluoroacetate
-
inhibits a later step of the electron flow as it binds to the ubiquinone docking sites and abrogates the transfer of electrons to this molecule. It causes a time- and dose-dependent increase of apoptosis. 20% inhibition at 0.5 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tcm62
-
importance in SDH assembly
-
additional information
-
stimulation of SIRT3 expression decreases the level of acetylation of the SdhA subunit and increases Complex II activity in kaempherol-treated cells compared to control and nicotinamide-treated cells
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.024
-
SQR activity in raji cells
0.039
-
SQR activity in HT-29 cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene SDHB; subunit B encoding gene SDHB
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
express only type II Fp subunit of SQR complex
Manually annotated by BRENDA team
-
epithelium
Manually annotated by BRENDA team
-
expression of 2 distinct flavoprotein subunits
Manually annotated by BRENDA team
-
CD4+
Manually annotated by BRENDA team
additional information
-
loss of SDH activity in chief cells is found in the majority, i.e. 90%, of head and neck paragaliomas
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
P31040; P21912; Q99643; O14521
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
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SDHB_HUMAN
280
0
31630
Swiss-Prot
Mitochondrion (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
P31040; P21912; Q99643; O14521
deacetylation modification of SDHA by SIRT3 (which is reversible by acetylation) increases the activity of SDH complex in mice and human chronic myelogenous leukemia cell lines (K562). SIRT3 is a member of the sirtuin family of NADP-dependent deacetylases in mitochondria which catalyses the deacetylation of various metabolic enzymes and components of oxidative phosphorylation including SDHA subunit. In line with this, acetylating compounds, in vitro, reduced the activity of SDH. Acetylation of the hydrophilic surface of SDHA may govern entrance of the substrate into the active site of the enzyme. Deacetylation also occurs in histones by histone deacetylases (HDACs). The inhibition of class I HDACs results in higher expression of SDH and promotion of oxidative phosphorylation in skeletal muscles and adipose tissues. Accordingly, class I HDACs cause mitochondrial dysfunction by deregulation of complex I and II (SDH) in cardiomyocyte. Chidamide, a histone deacetylase inhibitor increases SDHA expression, which might have a therapeutic value, as a tumor suppressor, in multiple myeloma patients
phosphoprotein
P31040; P21912; Q99643; O14521
ROS mediates the activation of FGR tyrosine kinase which phosphorylates SDHA at Y604 and that this function of FGR is required for the adjustment of metabolism under various conditions such as nutrient restriction, hypoxia/reoxygenation, and T-cell activation. This regulation together with the function of phagosomal NADPH oxidase (a source of ROS generation) seems to be essential for the activation of anti-bacterial response in macrophages through committing complex I and II (SDH) to respiration rather than their assembly. Additional to FGR, c-Src is another mitochondrial tyrosine kinase which targets both NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr193 of respiratory complex I and SDHA at Tyr215 of complex II. NDUFV2 phosphorylation is required for NADH dehydrogenase activity, which affects both respiration and cellular ATP content. SDHA phosphorylation, on the other hand, does not alter the enzyme activity but disconcerts electron transfer resulting in the generation of reactive oxygen species. The T98G cell line and the primary neurons expressing the mutants at the corresponding Tyr residues loose viability. These observations thus propound that the mitochondrial c-Src modulates oxidative phosphorylation by phosphorylating two respiratory components and that c-Src activity is essential for cell viability. Dephosphorylation of SDHA is exemplified by PTEN-like mitochondrial phosphatase-1 (PTPMT1), an enzyme which dephosphorylates phosphatidylglycerol phosphate (in cardiolipin biogenesis pathway) and SDHA. Inhibition of PTPMT1 leads to enhanced phosphorylation and activation of SDH and consequently lower glucose concentration. Increased SDH activity lowers glucose levels by at least two mechanisms, by inducing glucose uptake and by boosting the rate of glucose utilization. Collectively these results suggest that PTPMT1 is a major coordinator of glucose utilization by mitochondria
side-chain modification
-
reversible acetylation of SdhA reduces the enzyme activity, activation by deacetylation by SIRT3
succinylation
P31040; P21912; Q99643; O14521
the posttranslational modification converts the cationic lysine side chain to an anion with diverse implications for protein structure and function. Systematic profiling of the mammalian succinylome, identifies SDHA and SDHB as two succinylated proteins. Most of the succinylation sites identified across the succinylome have no overlap with acetylation sites, suggesting differential regulation of succinylation and acetylation
additional information
P31040; P21912; Q99643; O14521
posttranslational modifications regulate SDH levels by 4 means: phosphorylation, deacetylation, succinylation and propionylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A3G
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
C191Y
-
a novel germline missense SDHB mutation (C191Y) in a patient affected by a glomus tumor is reported. The missense mutation hits an amino acid residue conserved from mammals to the yeast Saccharomyces cerevisiae. Histochemistry demonstrates that SDH activity is selectively absent in the patient tumor tissue
G12S
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
G148D
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
H145N
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
H50R
-
naturally occurring germline mutation of gene SDHD, phenotype, overview
L157X
-
the case of a novel SDHB mutation (L157X) in a Japanese patient with abdominal paraganglioma following malignant lung metastasis is reported. Novel mutation is a nonsense mutation, resulting in a truncated protein. In addition, an asymptomatic carrier of the SDHB mutation in this family is identified
L85X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
R17X
-
naturally occuring mutation in the SDHD gene of a 29-year-old man showing metastases in both lungs and the liver, but no increased hormone production by the tumor, phenotype, overview
R46Q
-
a naturally occuring mutation in gene SDHB in a Japanese family with both abdominal and thoracic paraganglioma following metastasis
R46X
-
naturally ocurring mutations, the recurrent stop-codon mutation in succinate dehydrogenase subunit B gene might play a role in cellular pre-adaptation to hypoxia in normal peripheral blood and childhood T-cell acute leukemia, overview
S163P
-
naturally occurring germline mutation of gene SDHB, phenotype, overview
W61X
-
an unusual naturally occurring SDHC gene non-sense mutation in a case of laryngeal paraganglioma, phenotype with an additional thyroid papillary carcinoma, overview
Y114X
-
naturally occuring germline mutation of the subunit D encoding gene SDHD, the mutation is involved in metastatic paragangliomas development, phenotype
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit B encoding gene SDHB, DNA and amino acid sequence determination, genotyping, overview
bovine cDNA for the CII-3 subunit of complex II cloned into pUC118, cloning of complete cDNA using sequence information from the bovine clone, mapping of the succinate dehydrogenase C gene
-
cloning of 2 distinct cDNAs of flavoprotein subunit of SQR
-
DNA and amino acid sequence determination of mutated genes SDHB and SDHD from a Chinese family with the familial paraganglioma syndrome, pedigree of the family, overview
-
DNA and amino acid sequence determinatis of wild-type and germline mutants of the genes coding for the enzyme subunits SDHB, SDHC, and SDHD
-
gene SDHB ecoding the subunit B, genotype-phenotype correlations among patients with SDHB mutations in different exons do not reveal obvious differences for age at presentation, biochemical phenotype, primary tumor size and location, distribution of metastatic lesions, or presence of additional head and neck paragangliomas, overview
-
gene SDHB, chromoslomal location at 1p36.13, DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes
-
gene SDHD, DNA and amino acid sequence determination and analysis of wild-type and mutant genes
-
gene SDHD, encoding the cybS subunit of the succinate dehydrogenase, mapps to chromosome 11q23, genotyping of native wild-type and mutant genes, overview
-
genes encoding subunits SdhC, SdhD, and SdhB are located at 1q21,11q23, and 1p35-36.1
-
genes SDHB, SDHC, and SDHD, DNA and amino acid sequence determination and analysis, genotyping
-
genes SDHC, SDHD, and SDHB, DNA and amino acid sequence determination and analysis, expression analysis in healthy individuals and in patients with Cowden and Cowden-like syndromes, the latter show PTEN mutations, overview
-
genes SDHD and SDHB, DNA and amino acid sequence determination of healthy individuals and patients with paraganglioma and phaeochromocytomas, several samples, overview
-
genes SDHD and SDHB, DNA and amino acid sequence determination of healthy individuals and patients with paraganglioma and phaeochromocytomas, several smaples, overview
-
subunit C encoding gene SDHC, DNA and amino acid sequence determination, genotyping, overview
subunit encoding genes SDHA, and SDHD, DNA and amino acid sequence determination, genotyping, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
1-(4-chlorophenyl)-benzo-2,5-quinone treatment decreases in the mRNA levels of succinate dehydrogenase (complex II) subunits C and D (sdhc and sdhd). The decrease in sdhc and sdhd expression is associated with a significant decrease in complex II activity and increase in mitochondrial levels of reactive oxygen species
-
both succinate dehydrogenase, SDH, and succinate:ubiquinone oxidoreductase, SQR, activity are markedly and equally downregulated when subunits SDHA and SDHB are targeted, and also when SDHC and SDHD are inhibited
-
low levels of NFR-1 downregulate SDHA and thereby SDH complex expression. This stabilizes HIF-1 and promotes its nuclear translocation and high expression of glucose transporters and heme oxygenase-1. Deacetylation also occurs in histones by histone deacetylases (HDACs). The inhibition of class I HDACs results in higher expression of SDH and promotion of oxidative phosphorylation in skeletal muscles and adipose tissues. Chidamide, a histone deacetylase inhibitor increases SDHA expression
P31040; P21912; Q99643; O14521
the nuclear respiratory factor-1 (NRF-1) induces SDH expression through binding to the gene promoters of SDHA and SDHD in the aerobic cardiomyocyte
P31040; P21912; Q99643; O14521
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Elbehti-Green, A.; Au, H.C.; Mascarello, J.T.; Ream-Robinson, D.; Scheffler, I.E.
Characterization of the human SDHC gene encoding one of the integral membrane proteins of succinate-quinone oxidoreductase in mitochondria
Gene
213
133-140
1998
Homo sapiens
Manually annotated by BRENDA team
Tomitsuka, E.; Goto, Y.; Taniwaki, M.; Kita, K.
Direct evidence for expression of type II flavoprotein subunit in human complex II (succinate-ubiquinone reductase)
Biochem. Biophys. Res. Commun.
311
774-779
2003
Homo sapiens
Manually annotated by BRENDA team
Dekker, P.B.D.; Hogendoorn, P.C.W.; Kuipers-Dijkshoorn, N.; Prins, F.A.; van Duinen, S.G.; Taschner, P.E.M.; van der Mey, A.G.L.; Cornelisse, C.J.
SDHD mutations in head and neck paragangliomas result in destabilization of complex II in the mitochondrial respiratory chain with loss of enzymatic activity and abnormal mitochondrial morphology
J. Pathol.
201
480-486
2003
Homo sapiens
Manually annotated by BRENDA team
Ni, Y.; Zbuk, K.M.; Sadler, T.; Patocs, A.; Lobo, G.; Edelman, E.; Platzer, P.; Orloff, M.S.; Waite, K.A.; Eng, C.
Germline mutations and variants in the succinate dehydrogenase genes in Cowden and Cowden-like syndromes
Am. J. Hum. Genet.
83
261-268
2008
Homo sapiens
Manually annotated by BRENDA team
Timmers, H.J.; Pacak, K.; Bertherat, J.; Lenders, J.W.; Duet, M.; Eisenhofer, G.; Stratakis, C.A.; Niccoli-Sire, P.; Tran, B.H.; Burnichon, N.; Gimenez-Roqueplo, A.P.
Mutations associated with succinate dehydrogenase D-related malignant paragangliomas
Clin. Endocrinol. (Oxf.)
68
561-566
2008
Homo sapiens
Manually annotated by BRENDA team
Srirangalingam, U.; Walker, L.; Khoo, B.; Macdonald, F.; Gardner, D.; Wilkin, T.J.; Skelly, R.H.; George, E.; Spooner, D.; Monson, J.P.; Grossman, A.B.; Akker, S.A.; Pollard, P.J.; Plowman, N.; Avril, N.; Berney, D.M.; Burrin, J.M.; Reznek, R.H.; Kumar, V.K.; Maher, E.R.; Chew, S.L.
Clinical manifestations of familial paraganglioma and phaeochromocytomas in succinate dehydrogenase B gene mutation carriers
Clin. Endocrinol. (Oxf.)
69
587-596
2008
Homo sapiens
Manually annotated by BRENDA team
Takekoshi, K.; Isobe, K.; Suzuki, H.; Nissato, S.; Kawakami, Y.; Kawai, K.; Yamada, N.
R46Q mutation in the succinate dehydrogenase B gene (SDHB) in a Japanese family with both abdominal and thoracic paraganglioma following metastasis
Endocr. J.
55
299-303
2008
Homo sapiens
Manually annotated by BRENDA team
Zelinka, T.; Timmers, H.J.; Kozupa, A.; Chen, C.C.; Carrasquillo, J.A.; Reynolds, J.C.; Ling, A.; Eisenhofer, G.; Lazurova, I.; Adams, K.T.; Whatley, M.A.; Widimsky, J.; Pacak, K.
Role of positron emission tomography and bone scintigraphy in the evaluation of bone involvement in metastatic pheochromocytoma and paraganglioma: specific implications for succinate dehydrogenase enzyme subunit B gene mutations
Endocr. Relat. Cancer
15
311-323
2008
Homo sapiens
Manually annotated by BRENDA team
Pasini, B.; McWhinney, S.R.; Bei, T.; Matyakhina, L.; Stergiopoulos, S.; Muchow, M.; Boikos, S.A.; Ferrando, B.; Pacak, K.; Assie, G.; Baudin, E.; Chompret, A.; Ellison, J.W.; Briere, J.J.; Rustin, P.; Gimenez-Roqueplo, A.P.; Eng, C.; Carney, J.A.; Stratakis, C.A.
Clinical and molecular genetics of patients with the Carney-Stratakis syndrome and germline mutations of the genes coding for the succinate dehydrogenase subunits SDHB, SDHC, and SDHD
Eur. J. Hum. Genet.
16
79-88
2008
Homo sapiens
Manually annotated by BRENDA team
Papaspyrou, K.; Rossmann, H.; Fottner, C.; Weber, M.M.; Mann, W.; Lackner, K.J.; Helling, K.
Malignant paraganglioma caused by a novel germline mutation of the succinate dehydrogenase D-gene - a case report
Head Neck
30
964-969
2008
Homo sapiens
Manually annotated by BRENDA team
Ma, R.C.; Lam, C.W.; Chan, W.B.; So, W.Y.; Tong, S.F.; Chow, C.C.; Cockram, C.S.
A Chinese family with familial paraganglioma syndrome due to succinate dehydrogenase deficiency
Hong Kong Med. J.
13
151-154
2007
Homo sapiens
Manually annotated by BRENDA team
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
Byun, H.O.; Kim, H.Y.; Lim, J.J.; Seo, Y.H.; Yoon, G.
Mitochondrial dysfunction by complex II inhibition delays overall cell cycle progression via reactive oxygen species production
J. Cell. Biochem.
104
1747-1759
2008
Homo sapiens
Manually annotated by BRENDA team
Havekes, B.; Corssmit, E.P.; Jansen, J.C.; van der Mey, A.G.; Vriends, A.H.; Romijn, J.A.
Malignant paragangliomas associated with mutations in the succinate dehydrogenase D gene
J. Clin. Endocrinol. Metab.
92
1245-1248
2007
Homo sapiens
Manually annotated by BRENDA team
Amar, L.; Baudin, E.; Burnichon, N.; Peyrard, S.; Silvera, S.; Bertherat, J.; Bertagna, X.; Schlumberger, M.; Jeunemaitre, X.; Gimenez-Roqueplo, A.P.; Plouin, P.F.
Succinate dehydrogenase B gene mutations predict survival in patients with malignant pheochromocytomas or paragangliomas
J. Clin. Endocrinol. Metab.
92
3822-3828
2007
Homo sapiens
Manually annotated by BRENDA team
Lima, J.; Feijao, T.; Ferreira da Silva, A.; Pereira-Castro, I.; Fernandez-Ballester, G.; Maximo, V.; Herrero, A.; Serrano, L.; Sobrinho-Simoes, M.; Garcia-Rostan, G.
High frequency of germline succinate dehydrogenase mutations in sporadic cervical paragangliomas in northern Spain: mitochondrial succinate dehydrogenase structure-function relationships and clinical-pathological correlations
J. Clin. Endocrinol. Metab.
92
4853-4864
2007
Homo sapiens
Manually annotated by BRENDA team
Timmers, H.J.; Kozupa, A.; Eisenhofer, G.; Raygada, M.; Adams, K.T.; Solis, D.; Lenders, J.W.; Pacak, K.
Clinical presentations, biochemical phenotypes, and genotype-phenotype correlations in patients with succinate dehydrogenase subunit B-associated pheochromocytomas and paragangliomas
J. Clin. Endocrinol. Metab.
92
779-786
2007
Homo sapiens
Manually annotated by BRENDA team
Pigny, P.; Vincent, A.; Cardot Bauters, C.; Bertrand, M.; de Montpreville, V.T.; Crepin, M.; Porchet, N.; Caron, P.
Paraganglioma after maternal transmission of a succinate dehydrogenase gene mutation
J. Clin. Endocrinol. Metab.
93
1609-1615
2008
Homo sapiens
Manually annotated by BRENDA team
Garrel, R.; Raynaud, P.; Raingeard, I.; Muyshondt, C.; Gardiner, Q.; Guerrier, B.; Pujol, P.; Coupier, I.
An unusual succinate dehydrogenase gene mutation C in a case of laryngeal paraganglioma
J. Laryngol. Otol.
2008
1-4
2008
Homo sapiens
Manually annotated by BRENDA team
Hargreaves, I.P.; Duncan, A.J.; Wu, L.; Agrawal, A.; Land, J.M.; Heales, S.J.
Inhibition of mitochondrial complex IV leads to secondary loss complex II-III activity: implications for the pathogenesis and treatment of mitochondrial encephalomyopathies
Mitochondrion
7
284-287
2007
Homo sapiens
Manually annotated by BRENDA team
MacKenzie, E.D.; Selak, M.A.; Tennant, D.A.; Payne, L.J.; Crosby, S.; Frederiksen, C.M.; Watson, D.G.; Gottlieb, E.
Cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia in succinate dehydrogenase-deficient cells
Mol. Cell. Biol.
27
3282-3289
2007
Homo sapiens
Manually annotated by BRENDA team
Baysal, B.E.
A recurrent stop-codon mutation in succinate dehydrogenase subunit B gene in normal peripheral blood and childhood T-cell acute leukemia
PLoS ONE
2
e436
2007
Homo sapiens
Manually annotated by BRENDA team
Huang, K.T.; Dobrovic, A.; Fox, S.B.
No evidence for promoter region methylation of the succinate dehydrogenase and fumarate hydratase tumour suppressor genes in breast cancer
BMC Res. Notes
2
194
2009
Homo sapiens
Manually annotated by BRENDA team
Prasad, P.; Kant, J.A.; Wills, M.; OLeary, M.; Lovvorn, H.; Yang, E.
Loss of heterozygosity of succinate dehydrogenase B mutation by direct sequencing in synchronous paragangliomas
Cancer genet. Cytogenet.
192
82-85
2009
Homo sapiens
Manually annotated by BRENDA team
Richalet, J.P.; Gimenez-Roqueplo, A.P.; Peyrard, S.; Venisse, A.; Marelle, L.; Burnichon, N.; Bouzamondo, A.; Jeunemaitre, X.; Azizi, M.; Elghozi, J.L.
A role for succinate dehydrogenase genes in low chemoresponsiveness to hypoxia?
Clin. Auton. Res.
19
335-342
2009
Homo sapiens
Manually annotated by BRENDA team
Saito, T.; Saito, Y.; Matsumura, K.; Tsubota, Y.; Maniwa, T.; Kaneda, H.; Minami, K.; Sakaida, N.; Uemura, Y.; Kawa, G.; Yamamoto, N.; Fujii, Y.; Isobe, K.; Kawakami, Y.; Matsuda, T.; Takekoshi, K.
Novel mutation (L157X) in the succinate dehydrogenase B gene (SDHB) in a Japanese family with abdominal paraganglioma following lung metastasis
Endocr. J.
56
451-458
2009
Homo sapiens
Manually annotated by BRENDA team
He, J.; Makey, D.; Fojo, T.; Adams, K.T.; Havekes, B.; Eisenhofer, G.; Sullivan, P.; Lai, E.W.; Pacak, K.
Successful chemotherapy of hepatic metastases in a case of succinate dehydrogenase subunit B-related paraganglioma
Endocrine
36
189-193
2009
Homo sapiens
Manually annotated by BRENDA team
Goffrini, P.; Ercolino, T.; Panizza, E.; Giache, V.; Cavone, L.; Chiarugi, A.; Dima, V.; Ferrero, I.; Mannelli, M.
Functional study in a yeast model of a novel succinate dehydrogenase subunit B gene germline missense mutation (C191Y) diagnosed in a patient affected by a glomus tumor
Hum. Mol. Genet.
18
1860-1868
2009
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Cervera, A.M.; Bayley, J.P.; Devilee, P.; McCreath, K.J.
Inhibition of succinate dehydrogenase dysregulates histone modifications in mammalian cells
Mol. Cancer
8
89
2009
Homo sapiens
Manually annotated by BRENDA team
Cimen, H.; Han, M.J.; Yang, Y.; Tong, Q.; Koc, H.; Koc, E.C.
Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria
Biochemistry
49
304-311
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Rutter, J.; Winge, D.R.; Schiffman, J.D.
Succinate dehydrogenase - Assembly, regulation and role in human disease
Mitochondrion
10
393-401
2010
Homo sapiens
Manually annotated by BRENDA team
Lemarie, A.; Huc, L.; Pazarentzos, E.; Mahul-Mellier, A.L.; Grimm, S.
Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction
Cell Death Differ.
18
338-349
2011
Homo sapiens
Manually annotated by BRENDA team
Xiao, W.; Sarsour, E.H.; Wagner, B.A.; Doskey, C.M.; Buettner, G.R.; Domann, F.E.; Goswami, P.C.
Succinate dehydrogenase activity regulates PCB3-quinone-induced metabolic oxidative stress and toxicity in HaCaT human keratinocytes
Arch. Toxicol.
90
319-332
2016
Homo sapiens
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
Moosavi, B.; Berry, E.; Zhu, X.; Yang, W.; Yang, G.
The assembly of succinate dehydrogenase a key enzyme in bioenergetics
Cell. Mol. Life Sci.
76
4023-4042
2019
Homo sapiens (P31040 AND P21912 AND Q99643 AND O14521), Homo sapiens, Saccharomyces cerevisiae (Q00711 AND P21801 AND P33421 AND P37298)
Manually annotated by BRENDA team