Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (RSAD1)

Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (RSAD1) is a mitochondrial enzyme encoded by the RSAD1 gene in humans. It is classified as a member of the radical SAM superfamily of enzymes, predicted to facilitate reactions involving heme and porphyrin compounds, possibly acting as a heme chaperone or in an analogous pathway to oxygen-independent coproporphyrinogen-III oxidases seen in other species. RSAD1 binds iron–sulfur clusters and is localized to mitochondria. While expression profiles are catalogued across various tissues and in the context of cancer, there is currently no established evidence supporting its role as a therapeutic drug target, disease biomarker, or drug-interacting protein in clinical practice[2][4][5][6].

Other names

RSAD1Radical S-adenosyl methionine domain containing 1HemWPutative heme chaperoneOxygen-independent coproporphyrinogen-III oxidase-like protein RSAD1FLJ11164[2][6]