EC Number   |
General Information |
Reference |
|---|
   1.3.99.1 | malfunction |
mutation of Arg582 in Sdh1 precludes flavinylation as well as assembly of the tetrameric enzyme complex. Mutation of Arg638 compromises SDH function only when present in combination with a Cys630 substitution. Mutations of either Arg582 or Arg638/Cys630 do not markedly destabilize the Sdh1 polypeptide. The steady-state level of Sdh5 is markedly attenuated in the Sdh1 mutant cells. Truncation of its last 13 residues of Sdh1 abrogates this heme binding and renders the cells respiratory defective |
725497 |
| 1.3.99.1 | malfunction |
succinate production for the SDH-negative Saccharomyces cerevisiae is very low even under fully aerobic conditions, additional zinc finger proteins Mig1 and Mig2 deletion does not result in an increase in succinate production in the SDH-negative strain |
-, 724051 |
| 1.3.99.1 | malfunction |
when the Sl SDH2-2 gene is repressed by antisense RNA in a guard cellspecific manner, changes in neither stomatal aperture nor photosynthesis are observed. Antisense SDH transgenic tomato plants exhibit elevated aerial growth and fruit yield, growth phenotype, overview. Inhibition of succinate dehydrogenase results in a reduced flux through the TCA cycle |
726163 |
| 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 | 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 | metabolism |
the enzyme plays a key role in the regulation of aerobic respiration |
-, 723986 |
| 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 | more |
flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit, overview. SDH assembly appears to require FAD binding but not necessarily covalent FAD attachment. FAD binding is important to stabilize the Sdh1 conformation enabling association with Sdh2 and the membrane anchor subunits |
725497 |
| 1.3.99.1 | more |
protein SDHA F2 factor is needed for assembly and activity of SDH and also for normal root elongation, sequence diversity and conservation of SDHA F2 across kingdoms, phylogenetic analysis, overview |
726243 |
| 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 |
