ADH1C

From Wikipedia, the free encyclopedia


Alcohol dehydrogenase 1C (class I), gamma polypeptide
PDB rendering based on 1deh.
Available structures: 1deh, 1hdx, 1hdy, 1hdz, 1hso, 1hsz, 1ht0, 1htb, 1u3t, 1u3u, 1u3v, 1u3w, 3hud
Identifiers
Symbol(s) ADH1C; ADH3
External IDs OMIM: 103730 MGI87921 HomoloGene73888
Orthologs
Human Mouse
Entrez 126 11522
Ensembl n/a ENSMUSG00000074207
Uniprot n/a Q3UKA4
Refseq NM_000669 (mRNA)
NP_000660 (protein)
NM_007409 (mRNA)
NP_031435 (protein)
Location n/a Chr 3: 138.22 - 138.23 Mb
Pubmed search [1] [2]

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

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.[1]

[edit] References

[edit] Further reading

  • Smith M (1986). "Genetics of human alcohol and aldehyde dehydrogenases.". Adv. Hum. Genet. 15: 249–90. PMID 3006456. 
  • Seitz HK, Meier P (2007). "The role of acetaldehyde in upper digestive tract cancer in alcoholics.". Translational research : the journal of laboratory and clinical medicine 149 (6): 293–7. doi:10.1016/j.trsl.2006.12.002. PMID 17543846. 
  • Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features.". Biochemistry 15 (21): 4687–93. PMID 9982. 
  • Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R (1992). "Molecular structure of the human alcohol dehydrogenase 3 gene.". Jpn. J. Genet. 67 (2): 167–71. PMID 1524834. 
  • Hurley TD, Bosron WF, Hamilton JA, Amzel LM (1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.". Proc. Natl. Acad. Sci. U.S.A. 88 (18): 8149–53. PMID 1896463. 
  • Stewart MJ, McBride MS, Winter LA, Duester G (1990). "Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box.". Gene 90 (2): 271–9. PMID 2169444. 
  • Yasunami M, Kikuchi I, Sarapata D, Yoshida A (1990). "The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome.". Genomics 7 (2): 152–8. PMID 2347582. 
  • Tsukahara M, Yoshida A (1989). "Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization.". Genomics 4 (2): 218–20. PMID 2737681. 
  • Ikuta T, Szeto S, Yoshida A (1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.". Proc. Natl. Acad. Sci. U.S.A. 83 (3): 634–8. PMID 2935875. 
  • Xu YL, Carr LG, Bosron WF, et al. (1988). "Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification.". Genomics 2 (3): 209–14. PMID 3397059. 
  • Höög JO, Hedén LO, Larsson K, et al. (1986). "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.". Eur. J. Biochem. 159 (2): 215–8. PMID 3758060. 
  • Bühler R, Hempel J, Kaiser R, et al. (1985). "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain.". Eur. J. Biochem. 145 (3): 447–53. PMID 6391921. 
  • 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. PMID 7771649. 
  • Hurley TD, Bosron WF, Stone CL, Amzel LM (1994). "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.". J. Mol. Biol. 239 (3): 415–29. doi:10.1006/jmbi.1994.1382. PMID 8201622. 
  • Cheung C, Smith CK, Hoog JO, Hotchkiss SA (1999). "Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin.". Biochem. Biophys. Res. Commun. 261 (1): 100–7. doi:10.1006/bbrc.1999.0943. PMID 10405330. 
  • Duester G, Farrés J, Felder MR, et al. (1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family.". Biochem. Pharmacol. 58 (3): 389–95. PMID 10424757. 
  • Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD (2001). "Three-dimensional structures of the three human class I alcohol dehydrogenases.". Protein Sci. 10 (4): 697–706. PMID 11274460. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Osier MV, Pakstis AJ, Goldman D, et al. (2003). "A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans.". Alcohol. Clin. Exp. Res. 26 (12): 1759–63. doi:10.1097/01.ALC.0000042013.13899.75. PMID 12500098.