ADH1C
From Wikipedia, the free encyclopedia
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Alcohol dehydrogenase 1C (class I), gamma polypeptide
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| 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 MGI: 87921 HomoloGene: 73888 | |||||||||||||
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| 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) |
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| 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:. 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:. 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:. 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:. 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:. PMID 12500098.

