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Literature summary extracted from

  • Cervera, A.M.; Bayley, J.P.; Devilee, P.; McCreath, K.J.
    Inhibition of succinate dehydrogenase dysregulates histone modifications in mammalian cells (2009), Mol. Cancer, 8, 89.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.3.5.1 medicine mutations in the genes encoding succinate dehydrogenase are associated with hereditary predisposition to pheochromocytoma and paraganglioma. The results support the notion that loss of mitochondrial function alters epigenetic processes and might provide a signature methylation mark for paraganglioma Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 2-Thenoyltrifluoroacetone
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.5.1 HEK-293 cell
-
 Homo sapiens
-

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 succinate dehydrogenase
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.3.5.1 physiological function using pharmacological and siRNA methodologies it is shown that increased methylation of histone H3 is a general consequence of SDH loss-of-function in cultured mammalian cells and can be reversed by overexpression of the JMJD3 histone demethylase. ChIP analysis reveals that the core promoter of IGFBP7, which encodes a secreted protein upregulated after loss of SDHB, shows decreased occupancy by H3K27me3 (histone 3 methylated on residue K27) in the absence of SDH Homo sapiens