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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''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>
| update_page = yes  
 
| require_manual_inspection = no
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>
| update_protein_box = yes
 
| update_summary = yes
The human gene is located on [[chromosome 4]] in 4q22.
| update_citations = yes
 
}}
Previously ''ADH1B'' was called ''ADH2''.
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 ==
A [[single nucleotide polymorphism]] (SNP) in ''ADH1B'' is [[rs1229984]], that changes [[arginine]] to [[histidine]] at [[residue (chemistry)|residue]] 47.<ref>{{Cite journal
| author = Y. Matsuo | author-link = Y. Matsuo
| author2 = R. Yokoyama | author2-link = R. Yokoyama
| 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
| 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>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Role in pathology ==
{{GNF_Protein_box
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>
| image = PBB_Protein_ADH1B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1deh.
| PDB = {{PDB2|1deh}}, {{PDB2|1hdx}}, {{PDB2|1hdy}}, {{PDB2|1hdz}}, {{PDB2|1hso}}, {{PDB2|1hsz}}, {{PDB2|1ht0}}, {{PDB2|1htb}}, {{PDB2|1u3t}}, {{PDB2|1u3u}}, {{PDB2|1u3v}}, {{PDB2|1u3w}}, {{PDB2|3hud}}
| Name = Alcohol dehydrogenase IB (class I), beta polypeptide
| HGNCid = 250
| Symbol = ADH1B
| AltSymbols =; ADH2
| OMIM = 103720
| ECnumber = 
| Homologene = 88336
| MGIid = 
| Function = {{GNF_GO|id=GO:0004024 |text = alcohol dehydrogenase activity, zinc-dependent}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =  
| Process = {{GNF_GO|id=GO:0006069 |text = ethanol oxidation}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 125
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_000659
    | Hs_RefseqmRNA = NM_000668
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Alcohol dehydrogenase IB (class I), beta polypeptide''', also known as '''ADH1B''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==See also==
{{PBB_Summary
*[[Alcohol dehydrogenase]]
| section_title =  
*[[Aldehyde dehydrogenase]]
| summary_text = 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, hydroxysteroids, 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 = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=125| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ADH1B}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Smith M |title=Genetics of human alcohol and aldehyde dehydrogenases. |journal=Adv. Hum. Genet. |volume=15 |issue=  |pages= 249-90 |year= 1986 |pmid= 3006456 |doi=  }}
*{{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  | 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=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  | author=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=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  | author=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=  }}
*{{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  | author=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=  }}
*{{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  | author=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=  }}
*{{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  | author=Winter LA, Stewart MJ, Shean ML, ''et al.'' |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=  }}
*{{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  | author=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=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  | author=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=  }}
*{{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  | author=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=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  | author=Matsuo Y, Yokoyama R, Yokoyama S |title=The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide. |journal=Eur. J. Biochem. |volume=183 |issue= 2 |pages= 317-20 |year= 1989 |pmid= 2547609 |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  | author=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=  }}
*{{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  | author=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=  }}
*{{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  | author=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=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  | author=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=  }}
*{{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  | author=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=  }}
*{{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}}
*{{cite journal  | author=Hedén LO, Höög JO, Larsson K, ''et al.'' |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=  }}
*{{cite journal  | author=Xu YL, Carr LG, Bosron WF, ''et al.'' |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= }}
*{{cite journal  | author=Burnell JC, Carr LG, Dwulet FE, ''et al.'' |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=Biochem. Biophys. Res. Commun. |volume=146 |issue= 3 |pages= 1127-33 |year= 1987 |pmid= 3619918 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=125}}


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Revision as of 00:26, 27 October 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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Location (UCSC)n/an/a
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View/Edit Human

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

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, hydroxysteroids, 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.[2]

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

Previously ADH1B was called ADH2. 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.[3]

Variants

A single nucleotide polymorphism (SNP) in ADH1B is rs1229984, that changes arginine to histidine at residue 47.[4] 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.[5]

Another SNP is Arg369Cys.[6]

Role in pathology

A marked decrease of ADH1B mRNA was detected in corneal fibroblasts taken from persons suffering from keratoconus.[7]

See also

References

  1. ↑ Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249–90. doi:10.1007/978-1-4615-8356-1_5. PMID 3006456.
  2. ↑ "Entrez Gene: ADH1B alcohol dehydrogenase IB (class I), beta polypeptide".
  3. ↑ Sandra Porter (2008-08-21). "A gene by many other names and thoughts on teaching bioinformatics". ScienceBlogs. Archived from the original on 2009-02-15. Retrieved 2008-09-03.
  4. ↑ Y. Matsuo; R. Yokoyama & S. Yokoyama (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.
  5. ↑ T. Muramatsu; Z. C. Wang; Y. R. Fang; K. B. Hu; H. Yan; K. Yamada; S. Higuchi; S. Harada & H. Kono (August 1995). "Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai". Human Genetics. 96 (2): 151–154. doi:10.1007/BF00207371. PMID 7635462.
  6. ↑ J. C. Burnell; L. G. Carr; F. E. Dwulet; H. J. Edenberg; T. K. Li & W. F. Bosron (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.
  7. ↑ Mootha VV, Kanoff JM, Shankardas J, Dimitrijevich S (2009). "Marked reduction of alcohol dehydrogenase in keratoconus corneal fibroblasts". Mol. Vis. 15: 706–12. PMC 2666775. PMID 19365573.

External links

Further reading


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