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{{Infobox_gene}}
{{Infobox_gene}}
'''Alcohol dehydrogenase 1B''' is an [[enzyme]] that in humans is encoded by the ''ADH1B'' [[gene]].<ref name="pmid3006456">{{cite journal | author = Smith M | title = Genetics of human alcohol and aldehyde dehydrogenases | journal = Adv Hum Genet | volume = 15 | issue =  | pages = 249–90 |date=Mar 1986| pmid = 3006456 | pmc =  | doi = 10.1007/978-1-4615-8356-1_5}}</ref>
'''Alcohol dehydrogenase 1B''' is an [[enzyme]] that in humans is encoded by the ''ADH1B'' [[gene]].<ref name="pmid3006456">{{Cite book | vauthors = Smith M | title = Genetics of human alcohol and aldehyde dehydrogenases | journal = Advances in Human Genetics | volume = 15 | issue =  | pages = 249–90 | date = Mar 1986 | pmid = 3006456 | pmc =  | doi = 10.1007/978-1-4615-8356-1_5 | isbn = 978-1-4615-8358-5 }}</ref><ref>{{cite journal | vauthors = Hurley TD, Edenberg HJ | title = Genes encoding enzymes involved in ethanol metabolism | journal = Alcohol Research | volume = 34 | issue = 3 | pages = 339–44 | date = 2012 | pmid = 23134050 | pmc = 3756590 }}</ref>


The protein encoded by this gene 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, [[hydroxysteroid]]s, and [[lipid peroxidation]] products. This encoded protein, 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]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=125| accessdate = }}</ref>
The protein encoded by this gene is a member of the [[alcohol dehydrogenase]] family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol (beverage alcohol), [[retinol]], other aliphatic alcohols, [[hydroxysteroid]]s, and [[lipid peroxidation]] products. The encoded protein, known as ADH1B or beta-ADH, can form homodimers and heterodimers with ADH1A and ADH1C subunits, exhibits high activity for [[ethanol]] oxidation<ref>Hurley TD, Edenberg HJ, Bosron WF (1990). "Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47". J. Biol. Chem. 265 (27): 16366–72. {{PMID|2398055}}</ref><ref>{{cite journal | vauthors = Hurley TD, Edenberg HJ | title = Genes encoding enzymes involved in ethanol metabolism | journal = Alcohol Research | volume = 34 | issue = 3 | pages = 339–44 | date = 2012 | pmid = 23134050 | pmc = 3756590 }}</ref> and plays a major role in ethanol catabolism (oxidizing ethanol into acetaldehyde). The acetaldehyde is further metabolized to acetate by [[aldehyde dehydrogenase]] genes.  Three genes encoding the closely related alpha, beta and gamma subunits are tandemly organized in a genomic segment as a [[gene cluster]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=125| access-date = }}</ref>


The human gene is located on [[chromosome 4]] in 4q22.
The human gene is located on [[chromosome 4]] in 4q22.


Previously ''ADH1B'' was called ''ADH2''.
Previously ''ADH1B'' was called ''ADH2''. There are more genes in the family of alcohol dehydrogenase. These genes are now referred to as ''[[ADH1A]]'', ''[[ADH1C]]'', and ''[[ADH4]]'', ''[[ADH5]]'', ''[[ADH6]]'' and ''[[ADH7]]''.<ref>{{cite journal | vauthors = Hurley TD, Edenberg HJ | title = Genes encoding enzymes involved in ethanol metabolism | journal = Alcohol Research | volume = 34 | issue = 3 | pages = 339–44 | date = 2012 | pmid = 23134050 | pmc = 3756590 }}</ref>
There are more genes in the family of alcohol and [[aldehyde dehydrogenase]] genes.  
These genes are now referred to as ''[[ADH1A]]'', ''[[ADH1C]]'', and ''[[ADH4]]'', ''[[ADH5]]'', ''[[ADH6]]'' and ''[[ADH7]]''.<ref name="PorterS2008Gene">{{Cite web
|author=Sandra Porter
|author-link=Sandra Porter
|title=A gene by many other names and thoughts on teaching bioinformatics
|publisher=[[ScienceBlogs]]
|date=2008-08-21
|url=http://scienceblogs.com/digitalbio/2008/08/a_gene_by_any_other_name_and_t_1.php
|accessdate=2008-09-03
|deadurl=yes
|archiveurl=https://web.archive.org/web/20090215073648/http://scienceblogs.com/digitalbio/2008/08/a_gene_by_any_other_name_and_t_1.php
|archivedate=2009-02-15
}}</ref>


== Variants ==
== Variants ==
A [[single nucleotide polymorphism]] (SNP) in ''ADH1B'' is [[rs1229984]], that changes [[arginine]] to [[histidine]] at [[residue (chemistry)|residue]] 47.<ref>{{Cite journal
A [[single nucleotide polymorphism]] (SNP) in ''ADH1B'' is [[rs1229984]], that changes [[arginine]] to [[histidine]] at [[residue (chemistry)|residue]] 47 of the mature protein;<ref>{{cite journal | vauthors = Matsuo Y, Yokoyama R, Yokoyama S | title = The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide | journal = European Journal of Biochemistry | volume = 183 | issue = 2 | pages = 317–20 | date = August 1989 | pmid = 2547609 | doi = 10.1111/j.1432-1033.1989.tb14931.x }}</ref> standard nomenclature now includes the initiating methionine, so the position is officially 48.
| author = Y. Matsuo | author-link = Y. Matsuo
The 'typical' variant of this has been referred to as ADH2(1) or ADH2*1 while the 'atypical' has been referred to as, e.g., ADH2(2), ADH2*2, ADH1B*48His.
| author2 = R. Yokoyama | author2-link = R. Yokoyama
This SNP is associated with the risk for alcohol dependence, alcohol use disorders and alcohol consumption, with the atypical genotype having reduced risk of [[alcoholism]].<ref>{{cite journal | vauthors = Hurley TD, Edenberg HJ | title = Genes encoding enzymes involved in ethanol metabolism | journal = Alcohol Research | volume = 34 | issue = 3 | pages = 339–44 | date = 2012 | pmid = 23134050 | pmc = 3756590 }}</ref><ref>{{cite journal | vauthors = Thomasson HR, Edenberg HJ, Crabb DW, Mai XL, Jerome RE, Li TK, Wang SP, Lin YT, Lu RB, Yin SJ | title = Alcohol and aldehyde dehydrogenase genotypes and alcoholism in Chinese men | journal = American Journal of Human Genetics | volume = 48 | issue = 4 | pages = 677–81 | date = April 1991 | pmid = 2014795 | pmc = 1682953 }}</ref><ref>{{cite journal | vauthors = Bierut LJ, Goate AM, Breslau N, Johnson EO, Bertelsen S, Fox L, Agrawal A, Bucholz KK, Grucza R, Hesselbrock V, Kramer J, Kuperman S, Nurnberger J, Porjesz B, Saccone NL, Schuckit M, Tischfield J, Wang JC, Foroud T, Rice JP, Edenberg HJ | title = ADH1B is associated with alcohol dependence and alcohol consumption in populations of European and African ancestry | journal = Molecular Psychiatry | volume = 17 | issue = 4 | pages = 445–50 | date = April 2012 | pmid = 21968928 | pmc = 3252425 | doi = 10.1038/mp.2011.124 }}</ref>
| author3 = S. Yokoyama | author3-link = S. Yokoyama
| last-author-amp = yes
| title = The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide
| journal = [[European Journal of Biochemistry]]
| volume = 183
| issue = 2
| pages = 317–20
|date=August 1989
| pmid = 2547609
| doi = 10.1111/j.1432-1033.1989.tb14931.x
}}</ref>
The 'typical' variant of this has been referred to as ADH2(1) or ADH2*1 while the 'atypical' has been referred to as, e.g., ADH2(2), ADH2*2, ADH1B*47his, or ADH1B arg47-to-his.
This SNP may be related to alcohol consumption with the atypical genotype having reduced risk of [[alcoholism]].<ref>{{Cite journal
| author = T. Muramatsu | author-link = T. Muramatsu
| author2 = Z. C. Wang | author2-link = Z. C. Wang
| author3 = Y. R. Fang | author3-link = Y. R. Fang
| author4 = K. B. Hu | author4-link = K. B. Hu
| author5 = H. Yan | author5-link = H. Yan
| author6 = K. Yamada | author6-link = K. Yamada
| author7 = S. Higuchi | author7-link = S. Higuchi
| author8 = S. Harada | author8-link = S. Harada
| author9 = H. Kono | author9-link = H. Kono
| last-author-amp = yes
| title = Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai
| journal = [[Human Genetics (journal)|Human Genetics]]
| volume = 96
| issue = 2
| pages = 151–154
|date=August 1995
| pmid = 7635462
| doi = 10.1007/BF00207371
}}</ref>


Another SNP is [[Arg369Cys]].<ref>{{Cite journal
Another SNP is rs2066702 [Arg370Cys].<ref>{{cite journal | vauthors = Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF | title = The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding | journal = Biochemical and Biophysical Research Communications | volume = 146 | issue = 3 | pages = 1127–33 | date = August 1987 | pmid = 3619918 }}</ref> originally called position 369. This SNP is at high frequencies in populations from Africa, and also reduces risk for alcohol dependence<ref>{{Cite journal| vauthors = Walters RK, Adams MJ, Adkins AE, Aliev F, Bacanu SA, Batzler A, Bertelsen S, Biernacka J, Bigdeli TB, Chen LS, Clarke TK | display-authors = 6 |date=2018-03-10|title=Trans-ancestral GWAS of alcohol dependence reveals common genetic underpinnings with psychiatric disorders|url=https://www.biorxiv.org/content/early/2018/03/10/257311|journal=bioRxiv|language=en|pages=257311|doi=10.1101/257311}}</ref>.
| author = J. C. Burnell | author-link = J. C. Burnell
| author2 = L. G. Carr | author2-link = L. G. Carr
| author3 = F. E. Dwulet | author3-link = F. E. Dwulet
| author4 = H. J. Edenberg | author4-link = H. J. Edenberg
| author5 = T. K. Li | author5-link = T. K. Li
| author6 = W. F. Bosron | author6-link = W. F. Bosron
| last-author-amp = yes
| title = The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding
| journal = [[Biochemical and Biophysical Research Communications]]
| volume = 146
| issue = 3
| pages = 1127–33
|date=August 1987
| pmid = 3619918
}}</ref>


== Role in pathology ==
== Role in pathology ==
A marked decrease of ADH1B [[mRNA]] was detected in corneal [[fibroblast]]s taken from persons suffering from [[keratoconus]].<ref name="pmid19365573">{{cite journal |vauthors =Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S |title=Marked reduction of alcohol dehydrogenase in keratoconus corneal fibroblasts |journal=[[Mol. Vis.]] |volume=15 |issue= |pages=706–12 |year=2009 |pmid=19365573 |pmc=2666775 |doi= |url=}}</ref>
A marked decrease of ADH1B [[mRNA]] was detected in corneal [[fibroblast]]s taken from persons suffering from [[keratoconus]].<ref name="pmid19365573">{{cite journal | vauthors = Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S | title = Marked reduction of alcohol dehydrogenase in keratoconus corneal fibroblasts | journal = Molecular Vision | volume = 15 | issue = | pages = 706–12 | year = 2009 | pmid = 19365573 | pmc = 2666775 | doi = }}</ref>


==See also==
== See also ==
*[[Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase]]
*[[Aldehyde dehydrogenase]]
*[[Aldehyde dehydrogenase]]


==References==
== References ==
{{reflist}}
{{reflist}}


==External links==
== Further reading ==
* {{UCSC gene info|ADH1B}}
 
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Harada S | title = [Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese] | journal = Nihon Arukoru Yakubutsu Igakkai Zasshi = Japanese Journal of Alcohol Studies & Drug Dependence | volume = 36 | issue = 2 | pages = 85–106 | date = April 2001 | pmid = 11398342 | doi =  }}
| citations =
* {{cite journal | vauthors = Green RF, Stoler JM | title = Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview | journal = American Journal of Obstetrics and Gynecology | volume = 197 | issue = 1 | pages = 12–25 | date = July 2007 | pmid = 17618743 | doi = 10.1016/j.ajog.2007.02.028 }}
*{{cite journal | author=Harada S |title=[Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese] |journal=Nihon Arukōru Yakubutsu Igakkai zasshi (Japanese journal of alcohol studies & drug dependence) |volume=36 |issue= 2 |pages= 85–106 |year= 2001 |pmid= 11398342 |doi=  }}
* {{cite journal | vauthors = 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 | date = October 1976 | pmid = 9982 | doi = 10.1021/bi00666a023 }}
*{{cite journal | vauthors=Green RF, Stoler JM |title=Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview. |journal=Am. J. Obstet. Gynecol. |volume=197 |issue= 1 |pages= 12–25 |year= 2007 |pmid= 17618743 |doi= 10.1016/j.ajog.2007.02.028 }}
* {{cite journal | vauthors = 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 = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 18 | pages = 8149–53 | date = September 1991 | pmid = 1896463 | pmc = 52464 | doi = 10.1073/pnas.88.18.8149 }}
*{{cite journal | vauthors=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=10.1021/bi00666a023 }}
* {{cite journal | vauthors = 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 | date = June 1990 | pmid = 2169444 | doi = 10.1016/0378-1119(90)90190-3 }}
*{{cite journal | vauthors=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=10.1073/pnas.88.18.8149 | pmc=52464  }}
* {{cite journal | vauthors = Winter LA, Stewart MJ, Shean ML, Dong Y, Poellinger L, Okret S, Gustafsson JA, Duester G | title = A hormone response element upstream from the human alcohol dehydrogenase gene ADH2 consists of three tandem glucocorticoid receptor binding sites | journal = Gene | volume = 91 | issue = 2 | pages = 233–40 | date = July 1990 | pmid = 2210383 | doi = 10.1016/0378-1119(90)90093-7 }}
*{{cite journal | vauthors=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=10.1016/0378-1119(90)90190-3 }}
* {{cite journal | vauthors = Carr LG, Edenberg HJ | title = cis-acting sequences involved in protein binding and in vitro transcription of the human alcohol dehydrogenase gene ADH2 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 3 | pages = 1658–64 | date = January 1990 | pmid = 2295648 | doi =  }}
*{{cite journal | vauthors=Winter LA, Stewart MJ, Shean ML |title=A hormone response element upstream from the human alcohol dehydrogenase gene ADH2 consists of three tandem glucocorticoid receptor binding sites. |journal=Gene |volume=91 |issue= 2 |pages= 233–40 |year= 1990 |pmid= 2210383 |doi=10.1016/0378-1119(90)90093-7 |display-authors=etal}}
* {{cite journal | vauthors = 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 | date = June 1990 | pmid = 2347582 | doi = 10.1016/0888-7543(90)90535-3 }}
*{{cite journal | vauthors=Carr LG, Edenberg HJ |title=cis-acting sequences involved in protein binding and in vitro transcription of the human alcohol dehydrogenase gene ADH2. |journal=J. Biol. Chem. |volume=265 |issue= 3 |pages= 1658–64 |year= 1990 |pmid= 2295648 |doi=  }}
* {{cite journal | vauthors = Hurley TD, Edenberg HJ, Bosron WF | title = Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 27 | pages = 16366–72 | date = September 1990 | pmid = 2398055 | doi =  }}
*{{cite journal | vauthors=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=10.1016/0888-7543(90)90535-3 }}
* {{cite journal | vauthors = Carr LG, Xu Y, Ho WH, Edenberg HJ | title = Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit | journal = Alcoholism, Clinical and Experimental Research | volume = 13 | issue = 4 | pages = 594–6 | date = August 1989 | pmid = 2679216 | doi = 10.1111/j.1530-0277.1989.tb00383.x }}
*{{cite journal | vauthors=Hurley TD, Edenberg HJ, Bosron WF |title=Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47. |journal=J. Biol. Chem. |volume=265 |issue= 27 |pages= 16366–72 |year= 1990 |pmid= 2398055 |doi=  }}
* {{cite journal | vauthors = 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 | date = February 1989 | pmid = 2737681 | doi = 10.1016/0888-7543(89)90304-2 }}
*{{cite journal | vauthors=Carr LG, Xu Y, Ho WH, Edenberg HJ |title=Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. |journal=Alcohol. Clin. Exp. Res. |volume=13 |issue= 4 |pages= 594–6 |year= 1989 |pmid= 2679216 |doi=10.1111/j.1530-0277.1989.tb00383.x }}
* {{cite journal | vauthors = Duester G, Smith M, Bilanchone V, Hatfield GW | title = Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit | journal = The Journal of Biological Chemistry | volume = 261 | issue = 5 | pages = 2027–33 | date = February 1986 | pmid = 2935533 | doi =  }}
*{{cite journal | vauthors=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=10.1016/0888-7543(89)90304-2 }}
* {{cite journal | vauthors = Ikuta T, Szeto S, Yoshida A | title = Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 83 | issue = 3 | pages = 634–8 | date = February 1986 | pmid = 2935875 | pmc = 322918 | doi = 10.1073/pnas.83.3.634 }}
*{{cite journal | vauthors=Duester G, Smith M, Bilanchone V, Hatfield GW |title=Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. |journal=J. Biol. Chem. |volume=261 |issue= 5 |pages= 2027–33 |year= 1986 |pmid= 2935533 |doi=  }}
* {{cite journal | vauthors = Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A | title = Molecular cloning of a full-length cDNA for human alcohol dehydrogenase | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 82 | issue = 9 | pages = 2703–7 | date = May 1985 | pmid = 2986130 | pmc = 397633 | doi = 10.1073/pnas.82.9.2703 }}
*{{cite journal | vauthors=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=10.1073/pnas.83.3.634 | pmc=322918  }}
* {{cite journal | vauthors = Hedén LO, Höög JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jörnvall H, von Bahr-Lindström H | title = cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions | journal = FEBS Letters | volume = 194 | issue = 2 | pages = 327–32 | date = January 1986 | pmid = 3000832 | doi = 10.1016/0014-5793(86)80111-9 }}
*{{cite journal | vauthors=Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A |title=Molecular cloning of a full-length cDNA for human alcohol dehydrogenase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2703–7 |year= 1985 |pmid= 2986130 |doi=10.1073/pnas.82.9.2703 | pmc=397633  }}
* {{cite journal | vauthors = Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ | 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 | date = April 1988 | pmid = 3397059 | doi = 10.1016/0888-7543(88)90004-3 }}
*{{cite journal | vauthors=Hedén LO, Höög JO, Larsson K |title=cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. |journal=FEBS Lett. |volume=194 |issue= 2 |pages= 327–32 |year= 1986 |pmid= 3000832 |doi=10.1016/0014-5793(86)80111-9 |display-authors=etal}}
*{{cite journal | vauthors=Xu YL, Carr LG, Bosron WF |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=10.1016/0888-7543(88)90004-3 |display-authors=etal}}
}}
{{refend}}
{{refend}}
== External links ==
* {{UCSC gene info|ADH1B}}
{{PDB Gallery|geneid=125}}
{{PDB Gallery|geneid=125}}
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Latest revision as of 12:00, 10 January 2019

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Alcohol dehydrogenase 1B is an enzyme that in humans is encoded by the ADH1B gene.[1][2]

The protein encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol (beverage alcohol), retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein, known as ADH1B or beta-ADH, can form homodimers and heterodimers with ADH1A and ADH1C subunits, exhibits high activity for ethanol oxidation[3][4] and plays a major role in ethanol catabolism (oxidizing ethanol into acetaldehyde). The acetaldehyde is further metabolized to acetate by aldehyde dehydrogenase genes. Three genes encoding the closely related alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.[5]

The human gene is located on chromosome 4 in 4q22.

Previously ADH1B was called ADH2. There are more genes in the family of alcohol dehydrogenase. These genes are now referred to as ADH1A, ADH1C, and ADH4, ADH5, ADH6 and ADH7.[6]

Variants

A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47 of the mature protein;[7] standard nomenclature now includes the initiating methionine, so the position is officially 48. The 'typical' variant of this has been referred to as ADH2(1) or ADH2*1 while the 'atypical' has been referred to as, e.g., ADH2(2), ADH2*2, ADH1B*48His. This SNP is associated with the risk for alcohol dependence, alcohol use disorders and alcohol consumption, with the atypical genotype having reduced risk of alcoholism.[8][9][10]

Another SNP is rs2066702 [Arg370Cys].[11] originally called position 369. This SNP is at high frequencies in populations from Africa, and also reduces risk for alcohol dependence[12].

Role in pathology

A marked decrease of ADH1B mRNA was detected in corneal fibroblasts taken from persons suffering from keratoconus.[13]

See also

References

  1. ↑ Smith M (Mar 1986). Genetics of human alcohol and aldehyde dehydrogenases. Advances in Human Genetics. 15. pp. 249–90. doi:10.1007/978-1-4615-8356-1_5. ISBN 978-1-4615-8358-5. PMID 3006456.
  2. ↑ Hurley TD, Edenberg HJ (2012). "Genes encoding enzymes involved in ethanol metabolism". Alcohol Research. 34 (3): 339–44. PMC 3756590. PMID 23134050.
  3. ↑ Hurley TD, Edenberg HJ, Bosron WF (1990). "Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47". J. Biol. Chem. 265 (27): 16366–72. PMID 2398055
  4. ↑ Hurley TD, Edenberg HJ (2012). "Genes encoding enzymes involved in ethanol metabolism". Alcohol Research. 34 (3): 339–44. PMC 3756590. PMID 23134050.
  5. ↑ "Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide".
  6. ↑ Hurley TD, Edenberg HJ (2012). "Genes encoding enzymes involved in ethanol metabolism". Alcohol Research. 34 (3): 339–44. PMC 3756590. PMID 23134050.
  7. ↑ Matsuo Y, Yokoyama R, Yokoyama S (August 1989). "The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide". European Journal of Biochemistry. 183 (2): 317–20. doi:10.1111/j.1432-1033.1989.tb14931.x. PMID 2547609.
  8. ↑ Hurley TD, Edenberg HJ (2012). "Genes encoding enzymes involved in ethanol metabolism". Alcohol Research. 34 (3): 339–44. PMC 3756590. PMID 23134050.
  9. ↑ Thomasson HR, Edenberg HJ, Crabb DW, Mai XL, Jerome RE, Li TK, Wang SP, Lin YT, Lu RB, Yin SJ (April 1991). "Alcohol and aldehyde dehydrogenase genotypes and alcoholism in Chinese men". American Journal of Human Genetics. 48 (4): 677–81. PMC 1682953. PMID 2014795.
  10. ↑ Bierut LJ, Goate AM, Breslau N, Johnson EO, Bertelsen S, Fox L, Agrawal A, Bucholz KK, Grucza R, Hesselbrock V, Kramer J, Kuperman S, Nurnberger J, Porjesz B, Saccone NL, Schuckit M, Tischfield J, Wang JC, Foroud T, Rice JP, Edenberg HJ (April 2012). "ADH1B is associated with alcohol dependence and alcohol consumption in populations of European and African ancestry". Molecular Psychiatry. 17 (4): 445–50. doi:10.1038/mp.2011.124. PMC 3252425. PMID 21968928.
  11. ↑ Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF (August 1987). "The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding". Biochemical and Biophysical Research Communications. 146 (3): 1127–33. PMID 3619918.
  12. ↑ Walters RK, Adams MJ, Adkins AE, Aliev F, Bacanu SA, Batzler A, et al. (2018-03-10). "Trans-ancestral GWAS of alcohol dependence reveals common genetic underpinnings with psychiatric disorders". bioRxiv: 257311. doi:10.1101/257311.
  13. ↑ Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S (2009). "Marked reduction of alcohol dehydrogenase in keratoconus corneal fibroblasts". Molecular Vision. 15: 706–12. PMC 2666775. PMID 19365573.

Further reading

  • Harada S (April 2001). "[Classification of alcohol metabolizing enzymes and polymorphisms--specificity in Japanese]". Nihon Arukoru Yakubutsu Igakkai Zasshi = Japanese Journal of Alcohol Studies & Drug Dependence. 36 (2): 85–106. PMID 11398342.
  • Green RF, Stoler JM (July 2007). "Alcohol dehydrogenase 1B genotype and fetal alcohol syndrome: a HuGE minireview". American Journal of Obstetrics and Gynecology. 197 (1): 12–25. doi:10.1016/j.ajog.2007.02.028. PMID 17618743.
  • Lange LG, Sytkowski AJ, Vallee BL (October 1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features". Biochemistry. 15 (21): 4687–93. doi:10.1021/bi00666a023. PMID 9982.
  • Hurley TD, Bosron WF, Hamilton JA, Amzel LM (September 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 (June 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.
  • Winter LA, Stewart MJ, Shean ML, Dong Y, Poellinger L, Okret S, Gustafsson JA, Duester G (July 1990). "A hormone response element upstream from the human alcohol dehydrogenase gene ADH2 consists of three tandem glucocorticoid receptor binding sites". Gene. 91 (2): 233–40. doi:10.1016/0378-1119(90)90093-7. PMID 2210383.
  • Carr LG, Edenberg HJ (January 1990). "cis-acting sequences involved in protein binding and in vitro transcription of the human alcohol dehydrogenase gene ADH2". The Journal of Biological Chemistry. 265 (3): 1658–64. PMID 2295648.
  • Yasunami M, Kikuchi I, Sarapata D, Yoshida A (June 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.
  • Hurley TD, Edenberg HJ, Bosron WF (September 1990). "Expression and kinetic characterization of variants of human beta 1 beta 1 alcohol dehydrogenase containing substitutions at amino acid 47". The Journal of Biological Chemistry. 265 (27): 16366–72. PMID 2398055.
  • Carr LG, Xu Y, Ho WH, Edenberg HJ (August 1989). "Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit". Alcoholism, Clinical and Experimental Research. 13 (4): 594–6. doi:10.1111/j.1530-0277.1989.tb00383.x. PMID 2679216.
  • Tsukahara M, Yoshida A (February 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.
  • Duester G, Smith M, Bilanchone V, Hatfield GW (February 1986). "Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit". The Journal of Biological Chemistry. 261 (5): 2027–33. PMID 2935533.
  • Ikuta T, Szeto S, Yoshida A (February 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.
  • Ikuta T, Fujiyoshi T, Kurachi K, Yoshida A (May 1985). "Molecular cloning of a full-length cDNA for human alcohol dehydrogenase". Proceedings of the National Academy of Sciences of the United States of America. 82 (9): 2703–7. doi:10.1073/pnas.82.9.2703. PMC 397633. PMID 2986130.
  • Hedén LO, Höög JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jörnvall H, von Bahr-Lindström H (January 1986). "cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions". FEBS Letters. 194 (2): 327–32. doi:10.1016/0014-5793(86)80111-9. PMID 3000832.
  • Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ (April 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.

External links

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