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Chemical Compound Review

Accelerene     N,N-dimethyl-4-nitroso-aniline

Synonyms: Accelerine, NSC-2775, ACMC-1BT6K, CCRIS 3057, LS-808, ...
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Disease relevance of p-Nitrosodimethylaniline


High impact information on p-Nitrosodimethylaniline

  • N,N-Dimethyl-p-nitrosoaniline, mixed with the lipid in a molar ratio of 1.3:1, completely prevents the oxidation of lipid due to decomposing peroxychromate at pH 9.0, but some linoleic acid is lost if the incubation is done at pH 7 [3].
  • N,N-Dimethyl-p-nitrosoaniline was not metabolized by transketolase under the conditions employed for the other substrates [4].
  • Upon irradiation (lambda>500nm) of an oxygen-saturated aqueous solution of phycobiliproteins, particularly, C-phycocyanin (C-PC), allophycocyanin (APC) or R-phycoerythrin (R-PE), the formation of singlet oxygen (1O2) was detected by using imidazole in the presence of p-nitrosodimethylaniline (RNO) [5].
  • The steady-state kinetics of the enzyme modified by affinity labelling with NAD analogue, nicotinamide-N6-[N-(6-aminohexyl)carbamoylmethyl]-adenine dinucleotide, has been investigated using a recycling reaction with p-nitrosodimethylaniline and n-butanol as substrates and compared to the kinetics of native alcohol dehydrogenase [6].
  • The oxidation-promoting reactivity of the Cu(II)-sinefungin complex in the presence of hydrogen peroxide was studied at pH 7.4, using N,N-dimethyl-p-nitrosoaniline (NDMA), as well as plasmid DNA as target molecules [7].

Biological context of p-Nitrosodimethylaniline

  • Whole-of-life tests of the C-nitroso compounds p-nitrosodimethylaniline (NDMA) and p-nitroso-diethylaniline (NDEA) have been completed in male rats and mice fed maximum tolerated doses continuously over the first halves of their respective natural lifespans [8].

Associations of p-Nitrosodimethylaniline with other chemical compounds


Gene context of p-Nitrosodimethylaniline


  1. Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes. Schenkels, P., Duine, J.A. Microbiology (Reading, Engl.) (2000) [Pubmed]
  2. Molecular characterization of microbial alcohol dehydrogenases. Reid, M.F., Fewson, C.A. Crit. Rev. Microbiol. (1994) [Pubmed]
  3. Decomposing potassium peroxychromate produces hydroxyl radical (.OH) that can peroxidize the unsaturated fatty acids of phospholipid dispersions. Edwards, J.C., Quinn, P.J. J. Lipid Res. (1982) [Pubmed]
  4. Effect of ring substituents on the transketolase-catalyzed conversion of nitroso aromatics to hydroxamic acids. Corbett, M.D., Corbett, B.R. Biochem. Pharmacol. (1986) [Pubmed]
  5. Photosensitized formation of singlet oxygen by phycobiliproteins in neutral aqueous solutions. Zhang, S.P., Zhao, J.Q., Jiang, L.J. Free Radic. Res. (2000) [Pubmed]
  6. Steady-state kinetics of horse-liver alcohol dehydrogenase with a covalently bound coenzyme analogue. Kovár, J., Simek, K., Kucera, I., Matyska, L. Eur. J. Biochem. (1984) [Pubmed]
  7. Influence of the physiologically widespread substances on the oxidative activity of copper(II) complexes with sinefungin, a nucleoside antibiotic. Mucha, A., Cappanelli, M., Szczepanik, W., Kaczmarek, P., Skała, J., Jezowska-Bojczuk, M. J. Inorg. Biochem. (2006) [Pubmed]
  8. Oncogenicity tests of p-nitroso-N,N-dimethylaniline and p-nitroso-N,N-diethylaniline in NZR rats and NZO mice. Goodall, C.M., Lijinsky, W. Pathology. (1976) [Pubmed]
  9. Protection of UV-radiation induced skin toxicity by reactive oxygen scavengers. Ray, R.S., Joshi, P.C. Indian J. Exp. Biol. (1995) [Pubmed]
  10. Redox-elimination reaction catalyzed by yeast alcohol dehydrogenase. Trivić, S., Leskovac, V. Biochem. Int. (1991) [Pubmed]
  11. The activity of class I, II, III, and IV alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in colorectal cancer. Jelski, W., Zalewski, B., Chrostek, L., Szmitkowski, M. Dig. Dis. Sci. (2004) [Pubmed]
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