ADH1A: Difference between revisions

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Latest revision as of 12:06, 10 January 2019

Alcohol dehydrogenase 1A is an enzyme that in humans is encoded by the ADH1A gene.^[1]^[2]

This gene encodes class I alcohol dehydrogenase, alpha 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. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.^[2]

References

↑ 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. ISBN 978-1-4615-8358-5. PMID 3006456.
↑ ^2.0 ^2.1 "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide".

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.
van Ooij C, Snyder RC, Paeper BW, Duester G (1992). "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein". Mol. Cell. Biol. 12 (7): 3023–31. PMC 364516. PMID 1620113.
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.
Matsuo Y, Yokoyama S (1989). "Molecular structure of the human alcohol dehydrogenase 1 gene". FEBS Lett. 243 (1): 57–60. doi:10.1016/0014-5793(89)81217-7. PMID 2920825.
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. PMC 322918. PMID 2935875.
von Bahr-Lindström H, Höög JO, Hedén LO, et al. (1986). "cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase". Biochemistry. 25 (9): 2465–70. doi:10.1021/bi00357a026. PMID 3013304.
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.
Rodriguez-Zavala JS, Weiner H (2002). "Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation". Biochemistry. 41 (26): 8229–37. doi:10.1021/bi012081x. PMID 12081471.
Sandberg M, Yasar U, Strömberg P, et al. (2003). "Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase". British Journal of Clinical Pharmacology. 54 (4): 423–9. doi:10.1046/j.1365-2125.2002.01660.x. PMC 1874434. PMID 12392591.
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. PMC 139241. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Dannenberg LO, Chen HJ, Edenberg HJ (2006). "GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene". DNA Cell Biol. 24 (9): 543–52. doi:10.1089/dna.2005.24.543. PMID 16153155.
Jelski W, Chrostek L, Szmitkowski M (2007). "The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer". Pancreas. 35 (2): 142–6. doi:10.1097/MPA.0b013e318053eae2. PMID 17632320.

External links

Human ADH1A genome location and ADH1A gene details page in the UCSC Genome Browser.

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

[pmid3006456-1] 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. ISBN 978-1-4615-8358-5. PMID 3006456.

[entrez-2] 2.0 ^2.1 "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide".

[1]

[2]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Alcohol dehydrogenase 1A''' is an [[enzyme]] that in humans is encoded by the ''ADH1A'' [[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 | isbn = 978-1-4615-8358-5  }}</ref><ref name="entrez"/>
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-{{GNF_Protein_box
- | image = PBB_Protein_ADH1A_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 1A (class I), alpha polypeptide
- | HGNCid = 249
- | Symbol = ADH1A
- | AltSymbols =; ADH1
-  | OMIM = 103700
- | ECnumber =
- | Homologene = 88335
- | MGIid =
-  | GeneAtlas_image1 = PBB_GE_ADH1A_207820_at_tn.png
- | 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:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
-  | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
- | Process = {{GNF_GO|id=GO:0006066 |text = alcohol metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 124
-    | Hs_Ensembl = ENSG00000187758
-    | Hs_RefseqProtein = NP_000658
-    | Hs_RefseqmRNA = NM_000667
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 4
-    | Hs_GenLoc_start = 100416547
-    | Hs_GenLoc_end = 100431165
-    | Hs_Uniprot = P07327
-    | Mm_EntrezGene =
-    | Mm_Ensembl =
-    | Mm_RefseqmRNA =
-    | Mm_RefseqProtein =
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr =
-    | Mm_GenLoc_start =
-    | Mm_GenLoc_end =
-    | Mm_Uniprot =
-  }}
-}}
-'''Alcohol dehydrogenase 1A (class I), alpha polypeptide''', also known as '''ADH1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = This gene encodes class I alcohol dehydrogenase, alpha 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. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>
+| summary_text = This gene encodes class I alcohol dehydrogenase, alpha 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. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.<ref name="entrez">{{cite web | title = Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124| accessdate = }}</ref>
 }}
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | 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  | 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=van Ooij C, Snyder RC, Paeper BW, Duester G |title=Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 3023–31 |year= 1992 |pmid= 1620113 |doi=  | pmc=364516  }}
-*{{cite journal  | author=van Ooij C, Snyder RC, Paeper BW, Duester G |title=Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein. |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 3023-31 |year= 1992 |pmid= 1620113 |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=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=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=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=Matsuo Y, Yokoyama S |title=Molecular structure of the human alcohol dehydrogenase 1 gene |journal=FEBS Lett. |volume=243 |issue= 1 |pages= 57–60 |year= 1989 |pmid= 2920825 |doi=10.1016/0014-5793(89)81217-7  }}
-*{{cite journal  | author=Matsuo Y, Yokoyama S |title=Molecular structure of the human alcohol dehydrogenase 1 gene. |journal=FEBS Lett. |volume=243 |issue= 1 |pages= 57-60 |year= 1989 |pmid= 2920825 |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=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=von Bahr-Lindström H, Höög JO, Hedén LO |title=cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase |journal=Biochemistry |volume=25 |issue= 9 |pages= 2465–70 |year= 1986 |pmid= 3013304 |doi=10.1021/bi00357a026  |display-authors=etal}}
-*{{cite journal  | author=von Bahr-Lindström H, Höög JO, Hedén LO, ''et al.'' |title=cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. |journal=Biochemistry |volume=25 |issue= 9 |pages= 2465-70 |year= 1986 |pmid= 3013304 |doi=  }}
+*{{cite journal  | vauthors=Duester G, Farrés J, Felder MR |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389–95 |year= 1999 |pmid= 10424757 |doi=10.1016/S0006-2952(99)00065-9  |display-authors=etal}}
-*{{cite journal  | author=Duester G, Farrés J, Felder MR, ''et al.'' |title=Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family. |journal=Biochem. Pharmacol. |volume=58 |issue= 3 |pages= 389-95 |year= 1999 |pmid= 10424757 |doi=  }}
+*{{cite journal  | vauthors=Rodriguez-Zavala JS, Weiner H |title=Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation |journal=Biochemistry |volume=41 |issue= 26 |pages= 8229–37 |year= 2002 |pmid= 12081471 |doi=10.1021/bi012081x  }}
-*{{cite journal  | author=Rodriguez-Zavala JS, Weiner H |title=Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation. |journal=Biochemistry |volume=41 |issue= 26 |pages= 8229-37 |year= 2002 |pmid= 12081471 |doi=  }}
+*{{cite journal  | vauthors=Sandberg M, Yasar U, Strömberg P |title=Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase |journal=British Journal of Clinical Pharmacology |volume=54 |issue= 4 |pages= 423–9 |year= 2003 |pmid= 12392591 |doi=10.1046/j.1365-2125.2002.01660.x  | pmc=1874434  |display-authors=etal}}
-*{{cite journal  | author=Sandberg M, Yasar U, Strömberg P, ''et al.'' |title=Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase. |journal=British journal of clinical pharmacology |volume=54 |issue= 4 |pages= 423-9 |year= 2003 |pmid= 12392591 |doi=  }}
+*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  | vauthors=Dannenberg LO, Chen HJ, Edenberg HJ |title=GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene |journal=DNA Cell Biol. |volume=24 |issue= 9 |pages= 543–52 |year= 2006 |pmid= 16153155 |doi= 10.1089/dna.2005.24.543 }}
-*{{cite journal  | author=Dannenberg LO, Chen HJ, Edenberg HJ |title=GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene. |journal=DNA Cell Biol. |volume=24 |issue= 9 |pages= 543-52 |year= 2006 |pmid= 16153155 |doi= 10.1089/dna.2005.24.543 }}
+*{{cite journal  | vauthors=Jelski W, Chrostek L, Szmitkowski M |title=The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer |journal=Pancreas |volume=35 |issue= 2 |pages= 142–6 |year= 2007 |pmid= 17632320 |doi= 10.1097/MPA.0b013e318053eae2 }}
-*{{cite journal  | author=Jelski W, Chrostek L, Szmitkowski M |title=The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer. |journal=Pancreas |volume=35 |issue= 2 |pages= 142-6 |year= 2007 |pmid= 17632320 |doi= 10.1097/MPA.0b013e318053eae2 }}
 }}
 {{refend}}
+==External links==
+* {{UCSC gene info|ADH1A}}
+{{PDB Gallery|geneid=124}}
+<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{PBB_Controls
+| update_page = yes
+| require_manual_inspection = no
+| update_protein_box = yes
+| update_summary = yes
+| update_citations = yes
+}}
-{{protein-stub}}
+{{gene-4-stub}}
-{{WikiDoc Sources}}

ADH1A: Difference between revisions

Latest revision as of 12:06, 10 January 2019

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