Acyl-CoA dehydrogenase

Acyl-CoA dehydrogenase is a family of enzymes that function to catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. Substrate specificity is determined by the chain length of the acyl-CoA molecule. This enzyme has been linked to various metabolic disorders, including MCAD deficiency and SCAD deficiency.

Function

The primary function of Acyl-CoA dehydrogenase is to catalyze the initial step in each cycle of fatty acid β-oxidation in the mitochondria of cells. This involves the introduction of a trans double bond between C2 and C3 of the acyl-CoA molecule. The enzyme uses flavin adenine dinucleotide (FAD) as a cofactor.

Structure

Acyl-CoA dehydrogenase is a homotetramer with four identical subunits. Each subunit contains a FAD binding domain and an Acyl-CoA binding domain. The enzyme is active as a dimer of dimers and binds one molecule of FAD for each subunit.

Clinical significance

Mutations in the genes encoding for Acyl-CoA dehydrogenase can lead to metabolic disorders such as MCAD deficiency and SCAD deficiency. These disorders are characterized by the inability to metabolize certain types of fatty acids, leading to a buildup of these substances in the body.

See also

• Fatty acid metabolism
• Beta oxidation
• MCAD deficiency
• SCAD deficiency

References

Acyl-CoA dehydrogenase Resources
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