Aliases for ADH7 Gene
- Alcohol Dehydrogenase 7 (Class IV), Mu Or Sigma Polypeptide 2 3 5
- All-Trans-Retinol Dehydrogenase [NAD(+)] ADH7 3 4
- Alcohol Dehydrogenase Class IV Mu/Sigma Chain 3 4
- Alcohol Dehydrogenase Class 4 Mu/Sigma Chain 3 4
- Omega-Hydroxydecanoate Dehydrogenase ADH7 3 4
- Gastric Alcohol Dehydrogenase 3 4
- Retinol Dehydrogenase 3 4
- EC 126.96.36.199 4 51
- Class IV Sigmasigma Alcohol Dehydrogenase 3
External Ids for ADH7 Gene
Previous GeneCards Identifiers for ADH7 Gene
This gene encodes class IV alcohol dehydrogenase 7 mu or sigma subunit, which is 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 enzyme encoded by this gene is inefficient in ethanol oxidation, but is the most active as a retinol dehydrogenase; thus it may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. The expression of this gene is much more abundant in stomach than liver, thus differing from the other known gene family members. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2009]
GeneCards Summary for ADH7 Gene
ADH7 (Alcohol Dehydrogenase 7 (Class IV), Mu Or Sigma Polypeptide) is a Protein Coding gene. Diseases associated with ADH7 include Alcohol Dependence and Atrophic Gastritis. Among its related pathways are Glucose metabolism and Drug metabolism - cytochrome P450. Gene Ontology (GO) annotations related to this gene include oxidoreductase activity and retinol binding. An important paralog of this gene is ADH1A.
UniProtKB/Swiss-Prot Summary for ADH7 Gene
Catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis-retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid (PubMed:15369820, PubMed:16787387, PubMed:9600267). In vitro can also catalyzes the NADH-dependent reduction of all-trans-retinal and aldehydes and their derivatives (PubMed:15369820, PubMed:16787387, PubMed:9600267). Reduces preferentially all trans-retinal, all-trans-4-oxoretinal and hexanal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387, PubMed:15369820). Therefore may participate in retinoid metabolism, fatty acid omega-oxidation, and elimination of cytotoxic aldehydes produced by lipid peroxidation (PubMed:9600267, PubMed:15369820, PubMed:16787387).
Dehydrogenases are enzymes that catalyze reduction reactions through the transfer of hydrogen ions (protons) from the substrate to an acceptor or co-enzyme. Co-enzymes are small organic molecules involved in enzyme catalysis, such as nicotinamide adenine dinucleotide (NAD+ or NADH), nicotinamide adenine dinucleotide phosphate (NADP+ or NADPH), flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN).