ADH4
Description
The ADH4 (alcohol dehydrogenase 4 (class II), pi polypeptide) is a protein-coding gene located on chromosome 4.
The ADH4 gene encodes alcohol dehydrogenase 4, a member of the alcohol dehydrogenase enzyme family. This enzyme family is involved in the metabolism of various substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH4 is a homodimer composed of two pi subunits and exhibits high activity for oxidizing long-chain aliphatic and aromatic alcohols. It is less sensitive to pyrazole. This gene is located on chromosome 4 within a cluster of alcohol dehydrogenase genes. Evidence suggests that ADH4 originated in human ancestors approximately 10 million years ago, likely aiding them in utilizing rotting fruit as they transitioned to a terrestrial lifestyle.
ADH4 catalyzes the NAD-dependent oxidation of all-trans-retinol or 9-cis-retinol. It also oxidizes long-chain omega-hydroxy fatty acids like 20-HETE, producing the intermediate aldehyde 20-oxoarachidonate and the end product (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Additionally, ADH4 catalyzes the reduction of benzoquinones.
ADH4 is also known as ADH-2, HEL-S-4.
