Not only does it bind to RNA, AUH has also been observed to be involved in the metabolic enzymatic activity, making it a dual-role protein.

AUH has a similar fold that is found in other members of the enoyl-CoA hydratase/isomerase family; however, it is a hexamer as a dimer of trimers.

Between the two trimers of the enzyme, wide clefts were seen with a highly positive charge and lysine residues in alpha helix H1.

Localized in the mitochondria, AUH is responsible for the fifth step in the leucine degradation pathway and deficiencies in this enzyme's activity leads to a metabolic block in which 3-methylglutaconyl-CoA, accumulates in the mitochondrial matrix.

The lack of AUH is most impactful to the human body by causing 3-Methylglutaconic Acuduria Type 1, which is an autosomal recessive disorder of leucine degradation and can range in severity from developmental delay to slowly progressive leukoencephalopathy in adults.