ADH5 Antibody – Goat Polyclonal

This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene. [provided by RefSeq, Oct 2008]

ADH5: Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Protein type: Lipid Metabolism - fatty acid; Amino Acid Metabolism - tyrosine; Xenobiotic Metabolism - drug metabolism - cytochrome P450; EC 1.1.1.284; Oxidoreductase; Energy Metabolism - methane; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Cofactor and Vitamin Metabolism - retinol; EC 1.1.1.1; Mitochondrial; Xenobiotic Metabolism - metabolism by cytochrome P450

Chromosomal Location of Human Ortholog: 4q23

Cellular Component: cytosol; mitochondrion

Molecular Function: alcohol dehydrogenase activity; electron carrier activity; fatty acid binding; formaldehyde dehydrogenase activity; protein homodimerization activity; S-(hydroxymethyl)glutathione dehydrogenase activity; zinc ion binding

Biological Process: ethanol oxidation; formaldehyde catabolic process; peptidyl-cysteine S-nitrosylation; positive regulation of blood pressure; respiratory system process; response to lipopolysaccharide; response to nitrosative stress; response to redox state; retinoid metabolic process