ALDH3A1
Description
The ALDH3A1 (aldehyde dehydrogenase 3 family member A1) is a protein-coding gene located on chromosome 17.
ALDH3A1, the human gene encoding the enzyme aldehyde dehydrogenase, dimeric NADP-preferring, is responsible for oxidizing various aldehydes into their corresponding acids. This enzyme plays a vital role in detoxifying alcohol-derived acetaldehyde and in the metabolism of several important compounds like corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation products. ALDH3A1 forms a cytoplasmic homodimer that exhibits a preference for aromatic aldehyde substrates. Notably, the gene is located within the Smith–Magenis syndrome region on chromosome 17. ALDH3A1 is highly expressed in the cornea of mammals, constituting a significant portion (5-50%) of soluble protein content. However, its expression is virtually absent in the cornea of other vertebrates. The enzyme's structure is characterized by alpha helices, beta sheets, p-loop turns, and random coils, with the catalytic residue Cys244 located on an active site containing a Rossmann fold that binds the enzyme's cofactor, NAD(P)+. The catalytic mechanism of ALDH3A1 closely resembles that of other aldehyde dehydrogenase family members, involving a nucleophilic attack by the sulfur atom of Cys244 on the carbonyl group of the aldehyde substrate, leading to the release of a hydride ion.
ALDH3A1 plays a significant role in the detoxification of acetaldehyde, a byproduct of alcohol metabolism. It participates in the metabolism of various compounds, including corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation products. ALDH3A1 oxidizes medium and long chain aldehydes into harmless fatty acids. It preferentially oxidizes aromatic aldehyde substrates. ALDH3A1 comprises a significant portion (around 50%) of soluble proteins in corneal epithelial cells. It is suggested to contribute to the protection of the cornea from damage caused by ultraviolet light.
ALDH3A1 is also known as ALDH3, ALDHIII.
