ADH1C: Wikis

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Updated live from Wikipedia, last check: May 28, 2012 22:32 UTC (36 seconds ago)

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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

Symbols

ADH1C; ADH3

External IDs

OMIM: 103730 MGI: 87921 HomoloGene: 73888 GeneCards: ADH1C Gene

Gene ontology
Molecular function	• alcohol dehydrogenase activity, zinc-dependent • zinc ion binding • oxidoreductase activity • metal ion binding
Cellular component	• cytoplasm
Biological process	• alcohol metabolic process

Orthologs

Species

Human

Mouse

n/a

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

n/a

Chr 3:
138.22 - 138.23 Mb

PubMed search

[1]

[2]

Alcohol dehydrogenase 1C is an enzyme that in humans is encoded by the ADH1C gene.^[1]

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.^[2]

References

^ Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet 15: 249-90. PMID 3006456.
^ "Entrez Gene: ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=126.

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. doi:10.1021/bi00666a023. 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. doi:10.1266/jjg.67.167. 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. doi:10.1073/pnas.88.18.8149. 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. doi:10.1016/0378-1119(90)90190-3. 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. doi:10.1016/0888-7543(90)90535-3. 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. doi:10.1016/0888-7543(89)90304-2. 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. doi:10.1073/pnas.83.3.634. 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. doi:10.1016/0888-7543(88)90004-3. 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. doi:10.1111/j.1432-1033.1986.tb09855.x. 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. doi:10.1111/j.1432-1033.1984.tb08575.x. 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. doi:10.1111/j.1530-0277.1995.tb01490.x. 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. doi:10.1016/S0006-2952(99)00065-9. 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. doi:10.1110/ps.45001. 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.

PDB Gallery

1deh: CRYSTALLIZATION OF HUMAN BETA1 ALCOHOL DEHYDROGENASE (15 MG/ML) IN 50 MM SODIUM PHOSPHATE (PH 7.5), 2.0 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 OC, 13% (W/V) PEG 8000

1hdx: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hdy: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hdz: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A)

1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)

1ht0: HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE

1htb: CRYSTALLIZATION OF HUMAN BETA3 ALCOHOL DEHYDROGENASE (10 MG/ML) IN 100 MM SODIUM PHOSPHATE (PH 7.5), 7.5 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 C

1u3t: Crystal Structure of Human Alcohol Dehydrogenase Alpha-Alpha Isoform Complexed with N-Cyclopentyl-N-Cyclobutylformamide Determined to 2.5 Angstrom Resolution

1u3u: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Benzylformamide Determined to 1.6 Angstrom Resolution

1u3v: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Heptylformamide Determined to 1.65 Angstrom Resolution

1u3w: Crystal Structure of Human Alcohol Dehydrogenase Gamma-2-Gamma-2 Isoform Complexed with N-1-Methylheptylformamide Determined to 1.45 Angstrom Resolution