ADH6

Alcohol dehydrogenase 6 (class V), also known as ADH6, is a human gene.cite web | title = Entrez Gene: ADH6 alcohol dehydrogenase 6 (class V)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=130| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes class V alcohol dehydrogenase, 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. This gene is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5' UTR, which is a steroid hormone receptor binding site. The deduced amino acid sequence of the open reading frame of this gene shows about 60% positional identity with other known alcohol dehydrogenases. This gene may have a distinct physiologic function.cite web | title = Entrez Gene: ADH6 alcohol dehydrogenase 6 (class V)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=130| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lieber CS |title=Interaction of ethanol with drugs, hepatotoxic agents, carcinogens and vitamins. |journal=Alcohol Alcohol. |volume=25 |issue= 2-3 |pages= 157–76 |year= 1990 |pmid= 2198032 |doi=
*cite journal | author=Yoshida A |title=Genetic polymorphisms of alcohol metabolizing enzymes related to alcohol sensitivity and alcoholic diseases. |journal=Alcohol Alcohol. |volume=29 |issue= 6 |pages= 693–6 |year= 1995 |pmid= 7695785 |doi=
*cite journal | author=Chen CS, Yoshida A |title=Enzymatic properties of the protein encoded by newly cloned human alcohol dehydrogenase ADH6 gene. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 2 |pages= 743–7 |year= 1992 |pmid= 1755855 |doi=
*cite journal | author=Yasunami M, Chen CS, Yoshida A |title=A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7610–4 |year= 1991 |pmid= 1881901 |doi=
*cite journal | author=Zhi X, Chan EM, Edenberg HJ |title=Tissue-specific regulatory elements in the human alcohol dehydrogenase 6 gene. |journal=DNA Cell Biol. |volume=19 |issue= 8 |pages= 487–97 |year= 2000 |pmid= 10975466 |doi= 10.1089/10445490050128412
*cite journal | author=Strömberg P, Höög JO |title=Human class V alcohol dehydrogenase (ADH5): A complex transcription unit generates C-terminal multiplicity. |journal=Biochem. Biophys. Res. Commun. |volume=278 |issue= 3 |pages= 544–9 |year= 2001 |pmid= 11095947 |doi= 10.1006/bbrc.2000.3837
*cite journal | author=Osier MV, Pakstis AJ, Soodyall H, "et al." |title=A global perspective on genetic variation at the ADH genes reveals unusual patterns of linkage disequilibrium and diversity. |journal=Am. J. Hum. Genet. |volume=71 |issue= 1 |pages= 84–99 |year= 2002 |pmid= 12050823 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285

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