ADH1C
Alcohol dehydrogenase 1C is an enzyme that in humans is encoded by the ADH1C gene.[3]
Function
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.[4]
References
External links
Further reading
- Seitz HK, Meier P (Jun 2007). "The role of acetaldehyde in upper digestive tract cancer in alcoholics". Translational Research. 149 (6): 293–7. doi:10.1016/j.trsl.2006.12.002. PMID 17543846.
- Lange LG, Sytkowski AJ, Vallee BL (Oct 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 (Apr 1992). "Molecular structure of the human alcohol dehydrogenase 3 gene". Idengaku Zasshi. 67 (2): 167–71. doi:10.1266/jjg.67.167. PMID 1524834.
- Hurley TD, Bosron WF, Hamilton JA, Amzel LM (Sep 1991). "Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions". Proceedings of the National Academy of Sciences of the United States of America. 88 (18): 8149–53. doi:10.1073/pnas.88.18.8149. PMC 52464
. PMID 1896463.
- Stewart MJ, McBride MS, Winter LA, Duester G (Jun 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 (Jun 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 (Feb 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 (Feb 1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence". Proceedings of the National Academy of Sciences of the United States of America. 83 (3): 634–8. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875.
- Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (Apr 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, Jörnvall H, von Bahr-Lindström H (Sep 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". European Journal of Biochemistry / FEBS. 159 (2): 215–8. doi:10.1111/j.1432-1033.1986.tb09855.x. PMID 3758060.
- Bühler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jörnvall H (Dec 1984). "Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain". European Journal of Biochemistry / FEBS. 145 (3): 447–53. doi:10.1111/j.1432-1033.1984.tb08575.x. PMID 6391921.
- Cheung B, Anderson JK, Holmes RS, Beacham IR (Feb 1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis". Alcoholism: Clinical and Experimental Research. 19 (1): 185–6. doi:10.1111/j.1530-0277.1995.tb01490.x. PMID 7771649.
- Hurley TD, Bosron WF, Stone CL, Amzel LM (Jun 1994). "Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences". Journal of Molecular Biology. 239 (3): 415–29. doi:10.1006/jmbi.1994.1382. PMID 8201622.
- Cheung C, Smith CK, Hoog JO, Hotchkiss SA (Jul 1999). "Expression and localization of human alcohol and aldehyde dehydrogenase enzymes in skin". Biochemical and Biophysical Research Communications. 261 (1): 100–7. doi:10.1006/bbrc.1999.0943. PMID 10405330.
- Duester G, Farrés J, Felder MR, Holmes RS, Höög JO, Parés X, Plapp BV, Yin SJ, Jörnvall H (Aug 1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family". Biochemical Pharmacology. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757.
- Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD (Apr 2001). "Three-dimensional structures of the three human class I alcohol dehydrogenases". Protein Science. 10 (4): 697–706. doi:10.1110/ps.45001. PMC 2373965. PMID 11274460.
- Osier MV, Pakstis AJ, Goldman D, Edenberg HJ, Kidd JR, Kidd KK (Dec 2002). "A proline-threonine substitution in codon 351 of ADH1C is common in Native Americans". Alcoholism: Clinical and Experimental Research. 26 (12): 1759–63. doi:10.1097/01.ALC.0000042013.13899.75. PMID 12500098.
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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
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1hdx: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES
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1hdy: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES
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1hdz: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES
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1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A)
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1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)
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1ht0: HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE
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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
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1u3t: Crystal Structure of Human Alcohol Dehydrogenase Alpha-Alpha Isoform Complexed with N-Cyclopentyl-N-Cyclobutylformamide Determined to 2.5 Angstrom Resolution
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1u3u: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Benzylformamide Determined to 1.6 Angstrom Resolution
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1u3v: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Heptylformamide Determined to 1.65 Angstrom Resolution
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1u3w: Crystal Structure of Human Alcohol Dehydrogenase Gamma-2-Gamma-2 Isoform Complexed with N-1-Methylheptylformamide Determined to 1.45 Angstrom Resolution
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3hud: THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS
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