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Chemical Compound Review

ethanal     ethanal

Synonyms: aldehyde, ethanone, ACETALD, Acetaldehyd, Acetaldeyde, ...
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Disease relevance of acetaldehyde


Psychiatry related information on acetaldehyde

  • A mutation in the gene encoding for the liver mitochondrial aldehyde dehydrogenase (ALDH2-2), present in some Asian populations, lowers or abolishes the activity of this enzyme and results in elevations in blood acetaldehyde upon ethanol consumption, a phenotype that greatly protects against alcohol abuse and alcoholism [6].
  • Immunohistochemical demonstration of acetaldehyde-modified epitopes in human liver after alcohol consumption [7].
  • The data strongly suggest that genetic variation in both ADH and ALDH may influence drinking behavior and the risk of alcoholism developing through acetaldehyde formation [8].
  • Aldehyde excretion is influenced by numerous factors that affect the formation of lipid peroxides in vivo such as energy status, physical activity and environmental temperature, as well as by wide variations in the intake of peroxides in the diet [9].
  • BACKGROUND: The mutant allele of mitochondrial aldehyde dehydrogenase (ALDH2(*)2) was found to be associated with Alzheimer's disease (AD) in a Japanese sample, interacting with the apolipoprotein E epsilon 4 allele (Apo E4) [10].

High impact information on acetaldehyde


Chemical compound and disease context of acetaldehyde

  • This apparently contradictory finding is rationalized in terms of the subsequent enzymatic oxidation of acetaldehyde to acetic acid, which was previously regarded as the volatile fragment released by the action of the biosynthetic enzymes of Propionibacterium shermanii [14].
  • X-ray crystallographic data show that a specific tetrapeptide aldehyde inhibitor (N-acetylprolylalanylprolylphenylalaninal) forms a stable, covalent, tetrahedral addition complex with the serine protease, SGPA, from Streptomyces griseus [15].
  • The selective toxicity of cyclophosphamide is due, at least in part, to a greater expression of the relevant aldehyde dehydrogenase activity in normal cells relative to that expressed in certain tumor cells [16].
  • Measurement of activity and immunoblot results showed that ALDH2 and ATP synthase were also inhibited through oxidative modification of their cysteine or tyrosine residues in alcoholic fatty livers of rats [17].
  • When monocytes were treated with any type of IFN for 16 h, and then fixed with paraformaldehyde, they did not show cytotoxicity to A375 cells, but when they were fixed after treatment with norMDP or lipopolysaccharide they showed significant cytotoxicity to A375 melanoma cells [18].

Biological context of acetaldehyde


Anatomical context of acetaldehyde


Associations of acetaldehyde with other chemical compounds

  • Immunization with transition state analogue 1 results in a germline-encoded antibody that catalyses the rearrangement of hexadiene 2 to aldehyde 3 with a rate approaching that of a related pericyclic reaction catalysed by the enzyme chorismate mutase [26].
  • The antibodies use the epsilon-amino group of Lys to form an enamine with ketone substrates and use this enamine as a nascent carbon nucleophile to attack the second substrate, an aldehyde, to form a new carbon-carbon bond [27].
  • Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas [2].
  • Brefeldin A, gelonin, and a peptide aldehyde inhibitor of proteasomal processing each blocked presentation of macropinocytosed antigen, demonstrating that unusual access to the conventional class I MHC pathway was occurring [28].
  • DV-monocytes fixed with paraformaldehyde or glutaraldehyde, which produced no infectious virus, also induced high levels of IFN from PBL [29].
  • The second pathway is inducible and involves the microsomal ethanol-oxidizing system (MEOS), in which the oxidation of ethanol to acetaldehyde and acetic acid also leads to generation of reactive oxygen species (ROS) [30].

Gene context of acetaldehyde

  • Deficiency in mitochondrial aldehyde dehydrogenase (ALDH2), a tetrameric enzyme, results from inheriting one or two ALDH2*2 alleles [31].
  • Adding PON to HDL prolonged the oxidation lag phase and reduced HDL peroxide and aldehyde formation by up to 95% [32].
  • Here, we report the crystal structures of the 45-kDa catalytic domain of USP14 in isolation and in a complex with ubiquitin aldehyde, which reveal distinct structural features [33].
  • This screen yielded a number of genes not previously implicated in salt stress, including ALD6, which encodes an NADP(+)-dependent aldehyde dehydrogenase, and UTR1, which encodes an NAD+ kinase [34].
  • Ac-Tyr-Val-Ala-Asp-amino-4-methyl coumarin, patterned after site 2 of human pIL-1 beta, is a fluorogenic substrate for mICE, while the tetrapeptide aldehyde Ac-Tyr-Val-Ala-Asp-CHO is a potent inhibitor (Ki = 3 nM) that prevents generation and release of mature IL-1 beta by PECs (IC50 = 7 microM) [35].

Analytical, diagnostic and therapeutic context of acetaldehyde


  1. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Srivastava, S.K., Ramana, K.V., Bhatnagar, A. Endocr. Rev. (2005) [Pubmed]
  2. Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Romão, M.J., Archer, M., Moura, I., Moura, J.J., LeGall, J., Engh, R., Schneider, M., Hof, P., Huber, R. Science (1995) [Pubmed]
  3. Adenosine diphosphate effect on contractility of human muscle actomyosin: inhibition by ethanol and acetaldehyde. Puszkin, S., Rubin, E. Science (1975) [Pubmed]
  4. The rf2 nuclear restorer gene of male-sterile T-cytoplasm maize. Cui, X., Wise, R.P., Schnable, P.S. Science (1996) [Pubmed]
  5. Cytokines and arachidonic metabolites produced during human immunodeficiency virus (HIV)-infected macrophage-astroglia interactions: implications for the neuropathogenesis of HIV disease. Genis, P., Jett, M., Bernton, E.W., Boyle, T., Gelbard, H.A., Dzenko, K., Keane, R.W., Resnick, L., Mizrachi, Y., Volsky, D.J. J. Exp. Med. (1992) [Pubmed]
  6. Eliciting the low-activity aldehyde dehydrogenase Asian phenotype by an antisense mechanism results in an aversion to ethanol. Garver, E., Tu Gc, n.u.l.l., Cao, Q.N., Aini, M., Zhou, F., Israel, Y. J. Exp. Med. (2001) [Pubmed]
  7. Immunohistochemical demonstration of acetaldehyde-modified epitopes in human liver after alcohol consumption. Niemelä, O., Juvonen, T., Parkkila, S. J. Clin. Invest. (1991) [Pubmed]
  8. Polymorphism of alcohol and aldehyde dehydrogenase genes and alcoholic cirrhosis in Chinese patients. Chao, Y.C., Liou, S.R., Chung, Y.Y., Tang, H.S., Hsu, C.T., Li, T.K., Yin, S.J. Hepatology (1994) [Pubmed]
  9. Urinary aldehydes as indicators of lipid peroxidation in vivo. Draper, H.H., Csallany, A.S., Hadley, M. Free Radic. Biol. Med. (2000) [Pubmed]
  10. Assessment of association between mitochondrial aldehyde dehydrogenase polymorphism and Alzheimer's disease in an older Korean population. Kim, J.M., Stewart, R., Shin, I.S., Jung, J.S., Yoon, J.S. Neurobiol. Aging (2004) [Pubmed]
  11. Cytochrome P-4502E1: its physiological and pathological role. Lieber, C.S. Physiol. Rev. (1997) [Pubmed]
  12. Resurrecting ancestral alcohol dehydrogenases from yeast. Thomson, J.M., Gaucher, E.A., Burgan, M.F., De Kee, D.W., Li, T., Aris, J.P., Benner, S.A. Nat. Genet. (2005) [Pubmed]
  13. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.W., Gu, W., Cohen, R.E., Shi, Y. Cell (2002) [Pubmed]
  14. Biosynthesis of vitamin B12: concerning the identity of the two-carbon fragment eliminated during anaerobic formation of cobyrinic acid. Wang, J., Stolowich, N.J., Santander, P.J., Park, J.H., Scott, A.I. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  15. Crystallographic and kinetic investigations of the covalent complex formed by a specific tetrapeptide aldehyde and the serine protease from Streptomyces griseus. Brayer, G.D., Delbaere, L.T., James, M.N., Bauer, C.A., Thompson, R.C. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  16. Identification of the mouse aldehyde dehydrogenases important in aldophosphamide detoxification. Manthey, C.L., Landkamer, G.J., Sladek, N.E. Cancer Res. (1990) [Pubmed]
  17. Inactivation of oxidized and S-nitrosylated mitochondrial proteins in alcoholic fatty liver of rats. Moon, K.H., Hood, B.L., Kim, B.J., Hardwick, J.P., Conrads, T.P., Veenstra, T.D., Song, B.J. Hepatology (2006) [Pubmed]
  18. Membrane-associated interleukin 1 alpha as a mediator of tumor cell killing by human blood monocytes fixed with paraformaldehyde. Okubo, A., Sone, S., Tanaka, M., Ogura, T. Cancer Res. (1989) [Pubmed]
  19. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nicholson, D.W., Ali, A., Thornberry, N.A., Vaillancourt, J.P., Ding, C.K., Gallant, M., Gareau, Y., Griffin, P.R., Labelle, M., Lazebnik, Y.A. Nature (1995) [Pubmed]
  20. Visualization of dioxygen bound to copper during enzyme catalysis. Wilmot, C.M., Hajdu, J., McPherson, M.J., Knowles, P.F., Phillips, S.E. Science (1999) [Pubmed]
  21. Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2(2) allele is dominant. Crabb, D.W., Edenberg, H.J., Bosron, W.F., Li, T.K. J. Clin. Invest. (1989) [Pubmed]
  22. Does alcohol directly stimulate pancreatic fibrogenesis? Studies with rat pancreatic stellate cells. Apte, M.V., Phillips, P.A., Fahmy, R.G., Darby, S.J., Rodgers, S.C., McCaughan, G.W., Korsten, M.A., Pirola, R.C., Naidoo, D., Wilson, J.S. Gastroenterology (2000) [Pubmed]
  23. Suppression of hematopoietic-progenitor-cell proliferation by ethanol and acetaldehyde. Meagher, R.C., Sieber, F., Spivak, J.L. N. Engl. J. Med. (1982) [Pubmed]
  24. Acetaldehyde oxidation by hepatic mitochondria: decrease after chronic ethanol consumption. Hasumura, Y., Teschke, R., Lieber, C.S. Science (1975) [Pubmed]
  25. Ethyl alcohol enhances plasminogen activator secretion by endothelial cells. Laug, W.E. JAMA (1983) [Pubmed]
  26. The interplay between binding energy and catalysis in the evolution of a catalytic antibody. Ulrich, H.D., Mundorff, E., Santarsiero, B.D., Driggers, E.M., Stevens, R.C., Schultz, P.G. Nature (1997) [Pubmed]
  27. Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Wagner, J., Lerner, R.A., Barbas, C.F. Science (1995) [Pubmed]
  28. Class I MHC presentation of exogenous soluble antigen via macropinocytosis in bone marrow macrophages. Norbury, C.C., Hewlett, L.J., Prescott, A.R., Shastri, N., Watts, C. Immunity (1995) [Pubmed]
  29. Induction of interferon alpha from human lymphocytes by autologous, dengue virus-infected monocytes. Kurane, I., Ennis, F.A. J. Exp. Med. (1987) [Pubmed]
  30. Alcohol induced hepatic fibrosis: role of acetaldehyde. Mello, T., Ceni, E., Surrenti, C., Galli, A. Mol. Aspects Med. (2008) [Pubmed]
  31. The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases turnover of the enzyme tetramers in a dominant fashion. Xiao, Q., Weiner, H., Crabb, D.W. J. Clin. Invest. (1996) [Pubmed]
  32. Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase. Aviram, M., Rosenblat, M., Bisgaier, C.L., Newton, R.S., Primo-Parmo, S.L., La Du, B.N. J. Clin. Invest. (1998) [Pubmed]
  33. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. Hu, M., Li, P., Song, L., Jeffrey, P.D., Chenova, T.A., Wilkinson, K.D., Cohen, R.E., Shi, Y. EMBO J. (2005) [Pubmed]
  34. Identification of Ald6p as the target of a class of small-molecule suppressors of FK506 and their use in network dissection. Butcher, R.A., Schreiber, S.L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  35. Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a structurally conserved homologue of human IL-1 beta converting enzyme. Molineaux, S.M., Casano, F.J., Rolando, A.M., Peterson, E.P., Limjuco, G., Chin, J., Griffin, P.R., Calaycay, J.R., Ding, G.J., Yamin, T.T. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  36. A group specific anamnestic immune reaction against HIV-1 induced by a candidate vaccine against AIDS. Zagury, D., Bernard, J., Cheynier, R., Desportes, I., Leonard, R., Fouchard, M., Reveil, B., Ittele, D., Lurhuma, Z., Mbayo, K. Nature (1988) [Pubmed]
  37. Evidence against a role of acetaldehyde in electroencephalographic signs of ethanol-induced intoxication. Mikeska, J.A., Klemm, W.R. Science (1979) [Pubmed]
  38. Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload. Houglum, K., Filip, M., Witztum, J.L., Chojkier, M. J. Clin. Invest. (1990) [Pubmed]
  39. Protection of cats against progressive fibrosarcomas and persistent leukemia virus infection by vaccination with feline leukemia cells. Grant, C.K., de Noronha, F., Tusch, C., Michalek, M.T., McLane, M.F. J. Natl. Cancer Inst. (1980) [Pubmed]
  40. Morphological evaluation of opossum lower esophageal sphincter. Seelig, L.L., Goyal, R.K. Gastroenterology (1978) [Pubmed]
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