ADH7

Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide
PDB rendering based on 1agn.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AGN​, 1D1S​, 1D1T​
Identifiers
Symbols	ADH7 ; ADH4
External IDs	OMIM: 600086 MGI: 87926 HomoloGene: 37333 ChEMBL: 3867 GeneCards: ADH7 Gene
EC number	1.1.1.1
Gene ontology Molecular function • alcohol dehydrogenase (NAD) activity • alcohol dehydrogenase activity, zinc-dependent • aldehyde oxidase activity • retinol dehydrogenase activity • zinc ion binding • retinol binding • ethanol binding • receptor antagonist activity Cellular component • extracellular region • cytosol Biological process • retinoid metabolic process • ethanol catabolic process • ethanol oxidation • xenobiotic metabolic process • response to bacterium • fatty acid omega-oxidation • retinol metabolic process • retinoic acid metabolic process • small molecule metabolic process • response to ethanol • oxidation-reduction process • extracellular negative regulation of signal transduction Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	131	11529
Ensembl	ENSG00000196344	ENSMUSG00000055301
UniProt	P40394	Q64437
RefSeq (mRNA)	NM_000673	NM_009626
RefSeq (protein)	NP_000664	NP_033756
Location (UCSC)	Chr 4: 99.41 – 99.44 Mb	Chr 3: 138.22 – 138.23 Mb
PubMed search

Alcohol dehydrogenase class 4 mu/sigma chain is an enzyme that in humans is encoded by the ADH7 gene.^[1][2]

Function

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 makes it much more abundant in the stomach than the liver, thus it differs from the other known gene family members.^[2]

References

1. Satre MA, Zgombić-Knight M, Duester G (Jun 1994). "The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene". The Journal of Biological Chemistry 269 (22): 15606–12. PMID 8195208.
2. "Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide".

Further reading

• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD (Jul 1997). "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity". The Journal of Biological Chemistry 272 (30): 18558–63. doi:10.1074/jbc.272.30.18558. PMID 9228021.
• Yokoyama H, Baraona E, Lieber CS (Jan 1996). "Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH". Genomics 31 (2): 243–5. doi:10.1006/geno.1996.0040. PMID 8824810.
• Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R (Sep 1994). "Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)". FEBS Letters 351 (3): 411–5. doi:10.1016/0014-5793(94)00895-7. PMID 8082805.
• Yokoyama H, Baraona E, Lieber CS (Aug 1994). "Molecular cloning of human class IV alcohol dehydrogenase cDNA". Biochemical and Biophysical Research Communications 203 (1): 219–24. doi:10.1006/bbrc.1994.2170. PMID 8074657.
• Farrés J, Moreno A, Crosas B, Peralba JM, Allali-Hassani A, Hjelmqvist L, Jörnvall H, Parés X (Sep 1994). "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships". European Journal of Biochemistry / FEBS 224 (2): 549–57. doi:10.1111/j.1432-1033.1994.00549.x. PMID 7925371.
• Zgombić-Knight M, Foglio MH, Duester G (Mar 1995). "Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro". The Journal of Biological Chemistry 270 (9): 4305–11. doi:10.1074/jbc.270.9.4305. PMID 7876191.
• Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK (Feb 1995). "Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes". The Journal of Biological Chemistry 270 (8): 3625–30. doi:10.1074/jbc.270.8.3625. PMID 7876099.
• Cheung B, Anderson JK, Holmes RS, Beacham IR (Feb 1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis". Alcoholism: Clinical and Experimental Research 19 (1): 185–6. doi:10.1111/j.1530-0277.1995.tb01490.x. PMID 7771649.
• Parés X, Cederlund E, Moreno A, Saubi N, Höög JO, Jörnvall H (May 1992). "Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class". FEBS Letters 303 (1): 69–72. doi:10.1016/0014-5793(92)80479-Z. PMID 1592118.