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ADH7

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ADH7
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADH7, ADH4, alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide
External IDsOMIM: 600086; MGI: 87926; HomoloGene: 37333; GeneCards: ADH7; OMA:ADH7 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

131

11529

Ensembl

ENSG00000196344

ENSMUSG00000055301

UniProt

P40394

Q64437

RefSeq (mRNA)

NM_001166504
NM_000673

NM_009626

RefSeq (protein)

NP_000664
NP_001159976

NP_033756

Location (UCSC)Chr 4: 99.41 – 99.44 MbChr 3: 137.92 – 137.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alcohol dehydrogenase class 4 mu/sigma chain is an enzyme that in humans is encoded by the ADH7 gene.[5][6]

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.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196344 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000055301 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • 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.


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