Acyl-CoA dehydrogenase family member 11 (ACAD11)

Acyl-CoA dehydrogenase family member 11 (ACAD11) is a mitochondrial enzyme with a preference for oxidizing very long-chain fatty acids (C20–C26) and specialized 4-hydroxy fatty acid substrates, playing a critical role in β-oxidation and specialized lipid metabolism, particularly in the brain's white matter. ACAD11 possesses both an acyl-CoA dehydrogenase domain (utilizing FAD as a cofactor) and a kinase-like domain, a unique structure among the acyl-CoA dehydrogenases. Animal model studies and molecular analyses indicate that ACAD11 is essential for elimination of toxic 4-hydroxy acid lipids and maintaining cellular energy during metabolic stress, and its loss leads to aberrant lipid metabolism, including white adipose tissue accumulation. It is induced by p53, linking tumor metabolism to fatty acid oxidation pathways and cell survival under glucose deprivation. Alternative splicing generates multiple isoforms, with localization to mitochondria, peroxisomes, and possibly microsomes. No direct clinical targeting (drug or biomarker) is established, but its function suggests potential roles in neurological and metabolic disease.

Other names

ACAD-11FLJ12592ACD11_HUMANAcyl-Coenzyme A dehydrogenase family, member 11

Not applicable as no drugs are currently known to target this enzyme specifically. Mechanistically, generic inhibitors of β-oxidation or mitochondrial function would, in theory, impact ACAD11 enzymatic activity, but no validated ACAD11-selective mechanism is reported in the literature.