ACADL Human

ACADL is a mitochondrial flavoenzyme that requires flavin adenine dinucleotide (FAD) as a cofactor . It catalyzes the dehydrogenation of long-chain acyl-CoA substrates, introducing a trans double-bond between the C2 (α) and C3 (β) positions of the acyl-CoA thioester substrate . This reaction is the first step in the β-oxidation cycle, which ultimately breaks down fatty acids into acetyl-CoA, a key molecule in energy production .

The enzyme is specific for long-chain fatty acids, typically those with 8 to 18 carbon atoms . The human recombinant form of ACADL is produced using recombinant DNA technology, which allows for the expression of the human enzyme in a host organism, such as bacteria or yeast, for research and therapeutic purposes.

The gene encoding ACADL is located on chromosome 2 and is known by several aliases, including LCAD (Long-Chain Acyl-CoA Dehydrogenase) and ACAD4 . Mutations in the ACADL gene can lead to long-chain acyl-CoA dehydrogenase deficiency (LCADD), a metabolic disorder characterized by nonketotic hypoglycemia, muscle weakness, and cardiomyopathy . This condition results from the inability to properly oxidize long-chain fatty acids, leading to an accumulation of fatty acid intermediates and a deficiency in energy production.

Human recombinant ACADL is used extensively in biochemical research to study the mechanisms of fatty acid metabolism and the effects of genetic mutations on enzyme function. It is also employed in the development of diagnostic assays and potential therapeutic interventions for metabolic disorders related to fatty acid oxidation .