Aldehyde dehydrogenase 3 family, member A1
Aldehyde dehydrogenase, dimeric NADP-preferring is an enzyme that in humans is encoded by the ALDH3A1 gene.[1][2][3]
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.[3]
ALDH3A1 expression is notably high in the cornea of mammalian species, comprising from 5 to 50% of soluble protein content, but is almost absent from the cornea of other vertebrates.[4]
References
- ^ Hiraoka LR, Hsu L, Hsieh CL (Jul 1995). "Assignment of ALDH3 to human chromosome 17p11.2 and ALDH5 to human chromosome 9p13". Genomics 25 (1): 323–5. doi:10.1016/0888-7543(95)80150-K. PMID 7774944.
- ^ Hsu LC, Chang WC, Shibuya A, Yoshida A (Mar 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.
- ^ a b "Entrez Gene: ALDH3A1 aldehyde dehydrogenase 3 family, memberA1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=218.
- ^ Estey T, Piatigorsky J, Lassen N, Vasiliou V (January 2007). "ALDH3A1: a corneal crystallin with diverse functions". Exp. Eye Res. 84 (1): 3–12. doi:10.1016/j.exer.2006.04.010. PMID 16797007. http://linkinghub.elsevier.com/retrieve/pii/S0014-4835(06)00220-X.
Further reading
- Yoshida A (1993). "Molecular genetics of human aldehyde dehydrogenase.". Pharmacogenetics 2 (4): 139–47. doi:10.1097/00008571-199208000-00001. 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.
- 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. doi:10.1016/0014-5793(91)80559-L. 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. doi:10.1111/j.1469-1809.1985.tb01680.x. PMID 4073832.
- Teng YS (1981). "Stomach aldehyde dehydrogenase: report of a new locus.". Hum. Hered. 31 (2): 74–7. doi:10.1159/000153181. 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. doi:10.1111/j.1530-0277.1995.tb01525.x. PMID 7625577.
- 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1016/S0006-2952(97)00475-9. 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. PMC 1083732. PMID 11256614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083732.
- 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.
- 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. doi:10.1016/S0169-5002(02)00150-2. PMID 12367788.