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Beschreibung

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1, UniProt P21912, also known as Ip, Iron-sulfur subunit of complex II) is encoded by the SDHB (also known as IP, SDH, CWS2, PGL4, SDH1, SDHIP) gene (Gene ID 6390) in human. Originally described by Otto Warburg and now commonly known as the Warburg effect refers to the phenomenon that many tumor cells use aerobic glycolysis instead of mitochondrial respiration for energy production to support cell growth and proliferation. Enzymes involved in the complex network of metabolic pathways are therefore being studied as potential cancer markers and targets for treatment. Succinate dehydrogenase (SDH), also known as mitochondrial respiratory Complex II, is a holoenzyme consisting of four essential subunits, SDHA (a flavoprotein), SDHB (iron-sulfur protein), and two membrane anchor units SDHC and SDHD. SDH assembly requires two factors, SDHAF1 and SDHAF2, while its function is influenced by the deacetylase activity of SIRT3. SDH is the only enzyme complex known to participate in both the TCA cycle and electron transport chain (ETC.). SDH catalyzes the oxidation of succinate in the TCA to form fumarate, a reaction that is coupled to the reduction of ubiquinone to ubiquinol in the ETC. SDH loss-of-function mutations have been linked to pheochromocytoma (PCC), paraganglioma (PGL), gastrointestinal stromal tumor (GIST), renal cell carcinoma, and ovarian cancer.