ACADS Human

The ACAD family includes several enzymes that are categorized based on their specificity for short-, medium-, or long-chain fatty acid acyl-CoA substrates. Despite these differences, all ACADs share a common mechanism. They require flavin adenine dinucleotide (FAD) as a co-factor and an active site glutamate for their enzymatic activity .

The ACADS gene encodes the short-chain acyl-CoA dehydrogenase (SCAD), which is a tetrameric mitochondrial flavoprotein. This enzyme catalyzes the initial step of the mitochondrial fatty acid β-oxidation pathway . The human recombinant form of this enzyme is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 409 amino acids, with a molecular mass of 44 kDa .

ACADs have a dynamic evolutionary history, with their origins tracing back to the common ancestor of Archaea, Bacteria, and Eukaryota. This indicates their essential role in the metabolism of early life. The family has undergone numerous rounds of gene duplication, secondary losses, and lateral gene transfer events, leading to the diverse range of ACADs observed today .

In mammals, ACADs are vital for metabolizing fatty acids from ingested food materials. Deficiencies in these enzymes can lead to genetic disorders involving fatty acid oxidation, highlighting their importance in maintaining metabolic health .

Mutations in the ACADS gene can result in metabolic disorders such as Short-Chain Acyl-CoA Dehydrogenase Deficiency (SCADD). This condition can lead to a range of symptoms, including muscle weakness, hypoglycemia, and developmental delays. Understanding the structure and function of ACADs is crucial for developing therapeutic strategies for these disorders .

In summary, Acyl-Coenzyme A Dehydrogenase C-2 to C-3 (Human Recombinant) is a vital enzyme in the fatty acid β-oxidation pathway, with significant implications for metabolic health and disease.