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Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide
Protein ADH7 PDB 1agn.png
PDB rendering based on 1agn.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols ADH7 ; ADH4
External IDs OMIM600086 MGI87926 HomoloGene37333 ChEMBL: 3867 GeneCards: ADH7 Gene
EC number
RNA expression pattern
PBB GE ADH7 210505 at tn.png
More reference expression data
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:
100.33 – 100.36 Mb
Chr 3:
138.22 – 138.23 Mb
PubMed search [1] [2]

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

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]


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

Further reading[edit]

  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (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 et al. (1997). "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity". J. Biol. Chem. 272 (30): 18558–63. doi:10.1074/jbc.272.30.18558. PMID 9228021. 
  • Yokoyama H, Baraona E, Lieber CS (1997). "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 (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 (1994). "Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)". FEBS Lett. 351 (3): 411–5. doi:10.1016/0014-5793(94)00895-7. PMID 8082805. 
  • Yokoyama H, Baraona E, Lieber CS (1994). "Molecular cloning of human class IV alcohol dehydrogenase cDNA". Biochem. Biophys. Res. Commun. 203 (1): 219–24. doi:10.1006/bbrc.1994.2170. PMID 8074657. 
  • Farrés J, Moreno A, Crosas B et al. (1994). "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships". Eur. J. Biochem. 224 (2): 549–57. doi:10.1111/j.1432-1033.1994.00549.x. PMID 7925371. 
  • Zgombić-Knight M, Foglio MH, Duester G (1995). "Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro". J. Biol. Chem. 270 (9): 4305–11. doi:10.1074/jbc.270.9.4305. PMID 7876191. 
  • Kedishvili NY, Bosron WF, Stone CL et al. (1995). "Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes". J. Biol. Chem. 270 (8): 3625–30. doi:10.1074/jbc.270.8.3625. PMID 7876099. 
  • Cheung B, Anderson JK, Holmes RS, Beacham IR (1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis". Alcohol. Clin. Exp. Res. 19 (1): 185–6. doi:10.1111/j.1530-0277.1995.tb01490.x. PMID 7771649. 
  • Parés X, Cederlund E, Moreno A et al. (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 Lett. 303 (1): 69–72. doi:10.1016/0014-5793(92)80479-Z. PMID 1592118.