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Literature summary for 1.3.5.1 extracted from

  • Cimen, H.; Han, M.J.; Yang, Y.; Tong, Q.; Koc, H.; Koc, E.C.
    Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria (2010), Biochemistry, 49, 304-311.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
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 Mus musculus
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 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Mus musculus 5739
-
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification reversible acetylation of SdhA reduces the enzyme activity, activation by deacetylation by SIRT3 Homo sapiens
side-chain modification reversible acetylation of SdhA reduces the enzyme activity, activation by deacetylation by SIRT3. Acetylation of SdhA at conserved K179, K485, K498, and K538 residues, structure model, overview. Hyperacetylation of SdhA decreases Complex II activity in SIRT3 knockout mice Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
K-562 cell
-
Homo sapiens
-
liver
-
Mus musculus
-

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Mus musculus
7.2
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD bound in the succinate dehydrogenase flavoprotein, SdhA, subunit Mus musculus
FAD bound in the succinate dehydrogenase flavoprotein, SdhA, subunit Homo sapiens