ALDH3A1

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Aldehyde dehydrogenase 3 family, memberA1
Identifiers
Symbols ALDH3A1 ; ALDH3; ALDHIII; MGC10406
External IDs Template:OMIM5 Template:MGI HomoloGene20175
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Aldehyde dehydrogenase 3 family, memberA1, also known as ALDH3A1, is a human gene.[1]

Aldehyde dehydrogenases oxidize various aldehydes to the corresponding acids. They are involved in the detoxification of alcohol-derived acetaldehyde and in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. The enzyme encoded by this gene forms a cytoplasmic homodimer that preferentially oxidizes aromatic aldehyde substrates. The gene is located within the Smith-Magenis syndrome region on chromosome 17.[1]

References

  1. 1.0 1.1 "Entrez Gene: ALDH3A1 aldehyde dehydrogenase 3 family, memberA1".

Further reading

  • Yoshida A (1993). "Molecular genetics of human aldehyde dehydrogenase". Pharmacogenetics. 2 (4): 139–47. PMID 1306115.
  • Vasiliou V, Bairoch A, Tipton KF, Nebert DW (2000). "Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping". Pharmacogenetics. 9 (4): 421–34. PMID 10780262.
  • Hsu LC, Chang WC, Shibuya A, Yoshida A (1992). "Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli". J. Biol. Chem. 267 (5): 3030–7. PMID 1737758.
  • Eckey R, Timmann R, Hempel J; et al. (1991). "Biochemical, immunological, and molecular characterization of a "high Km" aldehyde dehydrogenase". Adv. Exp. Med. Biol. 284: 43–52. PMID 1905102.
  • Yin SJ, Vagelopoulos N, Wang SL, Jörnvall H (1991). "Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families". FEBS Lett. 283 (1): 85–8. PMID 2037078.
  • Santisteban I, Povey S, West LF; et al. (1986). "Chromosome assignment, biochemical and immunological studies on a human aldehyde dehydrogenase, ALDH3". Ann. Hum. Genet. 49 (Pt 2): 87–100. PMID 4073832.
  • Teng YS (1981). "Stomach aldehyde dehydrogenase: report of a new locus". Hum. Hered. 31 (2): 74–7. PMID 7228061.
  • Dyck LE (1995). "Polymorphism of a class 3 aldehyde dehydrogenase present in human saliva and in hair roots". Alcohol. Clin. Exp. Res. 19 (2): 420–6. PMID 7625577.
  • Hiraoka LR, Hsu L, Hsieh CL (1995). "Assignment of ALDH3 to human chromosome 17p11.2 and ALDH5 to human chromosome 9p13". Genomics. 25 (1): 323–5. PMID 7774944.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Hsu LC, Yoshida A (1993). "Human stomach aldehyde dehydrogenase, ALDH3". Adv. Exp. Med. Biol. 328: 141–52. PMID 8493892.
  • Rogers GR, Markova NG, De Laurenzi V; et al. (1997). "Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH)". Genomics. 39 (2): 127–35. doi:10.1006/geno.1996.4501. PMID 9027499.
  • Tsukamoto N, Chang C, Yoshida A (1997). "Mutations associated with Sjögren-Larsson syndrome". Ann. Hum. Genet. 61 (Pt 3): 235–42. doi:10.1046/j.1469-1809.1997.6130235.x. PMID 9250352.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Rekha GK, Devaraj VR, Sreerama L; et al. (1998). "Inhibition of human class 3 aldehyde dehydrogenase, and sensitization of tumor cells that express significant amounts of this enzyme to oxazaphosphorines, by chlorpropamide analogues". Biochem. Pharmacol. 55 (4): 465–74. PMID 9514081.
  • Simpson JC, Wellenreuther R, Poustka A; et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMID 11256614.
  • Rodriguez-Zavala JS, Weiner H (2002). "Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation". Biochemistry. 41 (26): 8229–37. PMID 12081471.
  • Yang M, Coles BF, Delongchamp R; et al. (2003). "Effects of the ADH3, CYP2E1, and GSTP1 genetic polymorphisms on their expressions in Caucasian lung tissue". Lung Cancer. 38 (1): 15–21. PMID 12367788.

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