EC Number   |
General Information |
Reference  |
|---|
   1.3.99.1 | more |
regulation of succinate dehydrogenase activity by SIRT3, a member of the sirtuin family of NAD+-dependent deacetylases, in mammalian mitochondria, the hydrophilic surface of SdhA may control the entry of the substrate into the active site of the protein and regulate the enzyme activity. The succinate dehydrogenase flavoprotein, SdhA, subunit is a substrate of SIRT3. 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 |
711232 |
| 1.3.99.1 | metabolism |
phytochrome A participates in the regulation of mitochondrial respiration through effect on SDH expression. White or red light are down-regulating factors for the mRNA content of the sdh1-2 and sdh2-3 genes and SDH catalytic activity both in wild-type plants and in the mutant deficient in the phytochrome B gene, but not in the mutant deficient in the phytochrome A gene, while the far red light of 730 nm reverses the red light effect |
712018 |
| 1.3.99.1 | physiological function |
SDH is located in the inner membrane of mitochondria and its activity is connected with the operation of the electron transport chain, where it functions as a succinate:ubiquinone reductase, EC 1.3.5.1 |
712018 |
| 1.3.99.1 | more |
compared to the wild type, the mutant sdhCAB deletion mutant DELTAsdh is impaired in planktonic growth under aerobic conditions, excreted acetic acid can not be reused and accumulated continuously. Succinate is excreted and found in the culture supernatant, and metabolome analysis with cells grown in chemically defined medium reveals reduced uptake/metabolism of some amino acids from the growth medium. Moreover, the mutant is able to counteract the steadily decreasing extracellular pH by increased urease activity. The addition of fumarate to the growth medium restored the wild-type phenotype. The mutant shows a small-colony variant-like phenotype, a slight increase in resistance to various aminoglycoside antibiotics, decreased pigmentation, and decreased growth under aerobic conditions due to the interruption of the TCA cycle, phenotype, overview |
-, 712296 |
| 1.3.99.1 | physiological function |
succinate dehydrogenase is part of the nonoxidative branch of the TCA cycle and is directly linked to the respiratory chain. This enzyme complex catalyzes the oxidation of succinate to fumarate, donating FADH2 for oxidative phosphorylation |
-, 712296 |
| 1.3.99.1 | metabolism |
SDH inhibition plays a role in metabolic suppression during hibernation and topor, overview. Oxaloacetate reversibly inhibits SDH in torpor, but cannot fully account for the drastic metabolic suppression observed during this hibernation phase. During arousal from the torpor phase of hibernation this suppression is reversed and metabolic rates rise dramatically |
712582 |
| 1.3.99.1 | physiological function |
SDH catalyzes the oxidation of succinate to fumarate in the matrix of the mitochondrion, donating electrons to ubiquinone that subsequently enter into the electron transport chain |
712582 |
| 1.3.99.1 | more |
the catalytic core Sdh1 and Sdh2 subunits contain the redox cofactors that participate in electron transfer to ubiquinone. Sdh1 contains the covalently bound FAD cofactor and the binding site for succinate. Sdh2 contains the three Fe-S centers that mediate electron transfer to ubiquinone in the complex of succinate-ubiquinone dehydrogenase, EC 1.3.5.1, regulation of SDH, overview. The Leigh syndrome, also known as subacute necrotizing encephalomyelopathy, is an early-onset progressive neurodegenerative disorder, associated with impaired SDH activity due to mutations, e.g. G555E, mechanism of the disease, overview. Mutations in SDHB,-C, and -D are asscoiated with tumor formation, overview |
712976 |
| 1.3.99.1 | more |
succinate dehydrogenase forms the peripheral part of the Succinate-ubiquinone oxidoreductase, EC 1.3.5.1, and is composed of a flavoprotein, SdhA, and an iron-sulfur protein, SdhB |
-, 713193 |
| 1.3.99.1 | metabolism |
the enzyme plays a key role in the regulation of aerobic respiration |
-, 723986 |
