ADH4
ADH4 (alcohol dehydrogenase 4, class II, pi polypeptide; also known as ADH-2) is a zinc-containing, NAD-dependent dehydrogenase that oxidises retinol and long-chain alcohols. It is the class II member of the alcohol dehydrogenase family. Browse Assay Genie's current range of ADH4 research reagents below, or read on for the biology behind the target.
ADH4 catalyses the NAD-dependent oxidation of all-trans-retinol and 9-cis-retinol. It also oxidises long-chain omega-hydroxy fatty acids such as 20-HETE, producing both the intermediate aldehyde 20-oxoarachidonate and the end product, the dicarboxylic acid (5Z,8Z,11Z,14Z)-eicosatetraenedioate. In addition, the enzyme catalyses the reduction of benzoquinones.
The ADH4 gene encodes the pi subunit of class II alcohol dehydrogenase, and the active enzyme is a homodimer of two pi subunits. Members of the alcohol dehydrogenase family metabolise a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids and lipid peroxidation products. Class II alcohol dehydrogenase shows high activity towards long-chain aliphatic and aromatic alcohols and is less sensitive to pyrazole. The ADH4 protein sits in the cytoplasm and belongs to the zinc-containing alcohol dehydrogenase family, class II subfamily.
The ADH4 gene lies on chromosome 4 within the cluster of alcohol dehydrogenase genes, alongside other class members such as ADH1A, ADH1B and ADH1C. HGNC lists it in the alcohol dehydrogenase gene group and records ADH-2 as an alias. Mouse and rat both carry an Adh4 ortholog, which supports comparative studies of retinoid and alcohol metabolism.
ADH4 oxidises all-trans-retinol and 9-cis-retinol using NAD, making it a relevant enzyme for studying how retinol is converted in the retinoid pathway.
The enzyme oxidises long-chain omega-hydroxy fatty acids such as 20-HETE to an aldehyde intermediate and a dicarboxylic acid end product.
As the class II pi subunit, ADH4 helps compare substrate preferences and pyrazole sensitivity across the clustered alcohol dehydrogenase genes.
ADH4 catalyses the reduction of benzoquinones, and the family handles aliphatic alcohols, hydroxysteroids and lipid peroxidation products.
ADH4 is an NAD-dependent enzyme that oxidises all-trans-retinol and 9-cis-retinol. It also oxidises long-chain omega-hydroxy fatty acids such as 20-HETE and catalyses the reduction of benzoquinones. Class II alcohol dehydrogenase is particularly active on long-chain aliphatic and aromatic alcohols.
The HGNC name is alcohol dehydrogenase 4 (class II), pi polypeptide, with ADH-2 as an alias. UniProt names the protein all-trans-retinol dehydrogenase [NAD(+)] ADH4. The active enzyme is a homodimer of two pi subunits, and its EC number is 1.1.1.105.
Yes. Mouse and rat each have an Adh4 ortholog. The human gene sits in a cluster of alcohol dehydrogenase genes on chromosome 4. Check the datasheet of any product for its validated reactivity.
Other alcohol dehydrogenase family members and related enzymes of alcohol and retinol metabolism.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P08319; product specifications from Assay Genie datasheets.