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Literature summary for 1.3.99.1 extracted from

  • Rutter, J.; Winge, D.R.; Schiffman, J.D.
    Succinate dehydrogenase - Assembly, regulation and role in human disease (2010), Mitochondrion, 10, 393-401.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining

General Information

General Information Comment Organism
additional information 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 Homo sapiens