ADH4

From Wikipedia, the free encyclopedia

Alcohol dehydrogenase 4 (class II), pi polypeptide

Identifiers

ADH4; ADH-2

External IDs

OMIM: 103740 MGI: 1349472 HomoloGene: 20162

Gene ontology
Molecular Function:	• alcohol dehydrogenase activity • electron-transferring-flavoprotein dehydrogenase activity • zinc ion binding • oxidoreductase activity • metal ion binding
Biological Process:	• alcohol metabolic process • ethanol oxidation • aldehyde metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000670 (mRNA)
NP_000661 (protein)

NM_011996 (mRNA)
NP_036126 (protein)

Location

Chr 4: 100.26 - 100.28 Mb

Chr 3: 138.35 - 138.37 Mb

Pubmed search

[1]

[2]

Alcohol dehydrogenase 4 (class II), pi polypeptide, also known as ADH4, is a human gene.^[1]

This gene encodes class II alcohol dehydrogenase 4 pi 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 II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.^[1]

[edit] References

^ ^a ^b Entrez Gene: ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide.

[edit] Further reading

Jörnvall H (1994). "The alcohol dehydrogenase system.". EXS 71: 221–9. PMID 8032153.
Edman K, Maret W (1993). "Alcohol dehydrogenase genes: restriction fragment length polymorphisms for ADH4 (pi-ADH) and ADH5 (chi-ADH) and construction of haplotypes among different ADH classes.". Hum. Genet. 90 (4): 395–401. PMID 1362387.
von Bahr-Lindström H, Jörnvall H, Höög JO (1991). "Cloning and characterization of the human ADH4 gene.". Gene 103 (2): 269–74. PMID 1889753.
Höög JO, von Bahr-Lindström H, Hedén LO, et al. (1987). "Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit.". Biochemistry 26 (7): 1926–32. PMID 3036213.
Mårdh G, Dingley AL, Auld DS, Vallee BL (1987). "Human class II (pi) alcohol dehydrogenase has a redox-specific function in norepinephrine metabolism.". Proc. Natl. Acad. Sci. U.S.A. 83 (23): 8908–12. PMID 3466164.
Li M, Edenberg HJ (1998). "Function of cis-acting elements in human alcohol dehydrogenase 4 (ADH4) promoter and role of C/EBP proteins in gene expression.". DNA Cell Biol. 17 (4): 387–97. PMID 9570155.
Tryggvason K, Romert A, Eriksson U (2001). "Biosynthesis of 9-cis-retinoic acid in vivo. The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases.". J. Biol. Chem. 276 (22): 19253–8. doi:10.1074/jbc.M100215200. PMID 11279029.
Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMID 11752456.
Iida A, Saito S, Sekine A, et al. (2002). "Thirteen single-nucleotide polymorphisms (SNPs) in the alcohol dehydrogenase 4 (ADH4) gene locus.". J. Hum. Genet. 47 (2): 74–6. PMID 11916005.
Strömberg P, Svensson S, Hedberg JJ, et al. (2002). "Identification and characterisation of two allelic forms of human alcohol dehydrogenase 2.". Cell. Mol. Life Sci. 59 (3): 552–9. PMID 11964133.
Chou CF, Lai CL, Chang YC, et al. (2002). "Kinetic mechanism of human class IV alcohol dehydrogenase functioning as retinol dehydrogenase.". J. Biol. Chem. 277 (28): 25209–16. doi:10.1074/jbc.M201947200. PMID 11997393.
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.
Galter D, Carmine A, Buervenich S, et al. (2003). "Distribution of class I, III and IV alcohol dehydrogenase mRNAs in the adult rat, mouse and human brain.". Eur. J. Biochem. 270 (6): 1316–26. PMID 12631290.
Neumark YD, Friedlander Y, Durst R, et al. (2004). "Alcohol dehydrogenase polymorphisms influence alcohol-elimination rates in a male Jewish population.". Alcohol. Clin. Exp. Res. 28 (1): 10–4. doi:10.1097/01.ALC.0000108667.79219.4D. PMID 14745297.
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. PMID 15489334.
Luo X, Kranzler HR, Zuo L, et al. (2006). "ADH4 gene variation is associated with alcohol and drug dependence: results from family controlled and population-structured association studies.". Pharmacogenet. Genomics 15 (11): 755–68. PMID 16220108.
Luo X, Kranzler HR, Zuo L, et al. (2006). "ADH4 gene variation is associated with alcohol dependence and drug dependence in European Americans: results from HWD tests and case-control association studies.". Neuropsychopharmacology 31 (5): 1085–95. doi:10.1038/sj.npp.1300925. PMID 16237392.
Luo X, Kranzler HR, Zuo L, et al. (2007). "Personality traits of agreeableness and extraversion are associated with ADH4 variation.". Biol. Psychiatry 61 (5): 599–608. doi:10.1016/j.biopsych.2006.05.017. PMID 17069770.