ADH1C

ADH1C

Alcohol dehydrogenase 1C (class I), gamma polypeptide, also known as ADH1C, is a human gene.

PBB_Summary
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summary_text = This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.cite web | title = Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Smith M |title=Genetics of human alcohol and aldehyde dehydrogenases. |journal=Adv. Hum. Genet. |volume=15 |issue= |pages= 249–90 |year= 1986 |pmid= 3006456 |doi=
*cite journal | author=Seitz HK, Meier P |title=The role of acetaldehyde in upper digestive tract cancer in alcoholics. |journal=Translational research : the journal of laboratory and clinical medicine |volume=149 |issue= 6 |pages= 293–7 |year= 2007 |pmid= 17543846 |doi= 10.1016/j.trsl.2006.12.002
*cite journal | author=Lange LG, Sytkowski AJ, Vallee BL |title=Human liver alcohol dehydrogenase: purification, composition, and catalytic features. |journal=Biochemistry |volume=15 |issue= 21 |pages= 4687–93 |year= 1976 |pmid= 9982 |doi=
*cite journal | author=Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R |title=Molecular structure of the human alcohol dehydrogenase 3 gene. |journal=Jpn. J. Genet. |volume=67 |issue= 2 |pages= 167–71 |year= 1992 |pmid= 1524834 |doi=
*cite journal | author=Hurley TD, Bosron WF, Hamilton JA, Amzel LM |title=Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 18 |pages= 8149–53 |year= 1991 |pmid= 1896463 |doi=
*cite journal | author=Stewart MJ, McBride MS, Winter LA, Duester G |title=Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box. |journal=Gene |volume=90 |issue= 2 |pages= 271–9 |year= 1990 |pmid= 2169444 |doi=
*cite journal | author=Yasunami M, Kikuchi I, Sarapata D, Yoshida A |title=The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. |journal=Genomics |volume=7 |issue= 2 |pages= 152–8 |year= 1990 |pmid= 2347582 |doi=
*cite journal | author=Tsukahara M, Yoshida A |title=Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization. |journal=Genomics |volume=4 |issue= 2 |pages= 218–20 |year= 1989 |pmid= 2737681 |doi=
*cite journal | author=Ikuta T, Szeto S, Yoshida A |title=Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 3 |pages= 634–8 |year= 1986 |pmid= 2935875 |doi=
*cite journal | author=Xu YL, Carr LG, Bosron WF, "et al." |title=Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. |journal=Genomics |volume=2 |issue= 3 |pages= 209–14 |year= 1988 |pmid= 3397059 |doi=
*cite journal | author=Höög JO, Hedén LO, Larsson K, "et al." |title=The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. |journal=Eur. J. Biochem. |volume=159 |issue= 2 |pages= 215–8 |year= 1986 |pmid= 3758060 |doi=
*cite journal | author=Bühler R, Hempel J, Kaiser R, "et al." |title=Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. |journal=Eur. J. Biochem. |volume=145 |issue= 3 |pages= 447–53 |year= 1985 |pmid= 6391921 |doi=
*cite journal | author=Cheung B, Anderson JK, Holmes RS, Beacham IR |title=Human stomach class IV alcohol dehydrogenase: molecular genetic analysis. |journal=Alcohol. Clin. Exp. Res. |volume=19 |issue= 1 |pages= 185–6 |year= 1995 |pmid= 7771649 |doi=
*cite journal | author=Hurley TD, Bosron WF, Stone CL, Amzel LM |title=Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. |journal=J. Mol. Biol. |volume=239 |issue= 3 |pages= 415–29 |year= 1994 |pmid= 8201622 |doi= 10.1006/jmbi.1994.1382
*cite journal | author=Cheung C, Smith CK, Hoog JO, Hotchkiss SA |title=Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin. |journal=Biochem. Biophys. Res. Commun. |volume=261 |issue= 1 |pages= 100–7 |year= 1999 |pmid= 10405330 |doi= 10.1006/bbrc.1999.0943
*cite journal | author=Duester G, Farrés J, Felder MR, "et al." |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family. |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389–95 |year= 1999 |pmid= 10424757 |doi=
*cite journal | author=Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD |title=Three-dimensional structures of the three human class I alcohol dehydrogenases. |journal=Protein Sci. |volume=10 |issue= 4 |pages= 697–706 |year= 2001 |pmid= 11274460 |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=Osier MV, Pakstis AJ, Goldman D, "et al." |title=A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans. |journal=Alcohol. Clin. Exp. Res. |volume=26 |issue= 12 |pages= 1759–63 |year= 2003 |pmid= 12500098 |doi= 10.1097/01.ALC.0000042013.13899.75

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