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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

AG-D-41709     N-(2-sulfanylethyl)ethanamide

Synonyms: ACMC-20ak7f, CHEBI:74410, CPD-10671, NSC-38835, LS-9810, ...
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High impact information on N-Acetyl cysteamin


Biological context of N-Acetyl cysteamin


Associations of N-Acetyl cysteamin with other chemical compounds


Gene context of N-Acetyl cysteamin

  • Using acyl-CoA substrates as acyl group donors and N-acetylcysteamine as the thiol acceptor, we devised a steady-state kinetic assay to probe the properties of these three didomain proteins and selected mutants [8].

Analytical, diagnostic and therapeutic context of N-Acetyl cysteamin

  • Active mutants were reassayed with (2R, S)-2-methyl-3-oxopentanoic acid N-acetylcysteamine thioester, and the alcohol products were analyzed by chiral HPLC [9].


  1. Expression and kinetic analysis of the substrate specificity of modules 5 and 6 of the picromycin/methymycin polyketide synthase. Yin, Y., Lu, H., Khosla, C., Cane, D.E. J. Am. Chem. Soc. (2003) [Pubmed]
  2. Directed mutagenesis alters the stereochemistry of catalysis by isolated ketoreductase domains from the erythromycin polyketide synthase. Baerga-Ortiz, A., Popovic, B., Siskos, A.P., O'Hare, H.M., Spiteller, D., Williams, M.G., Campillo, N., Spencer, J.B., Leadlay, P.F. Chem. Biol. (2006) [Pubmed]
  3. One-electron reduction of S-nitrosothiols in aqueous medium. Manoj, V.M., Mohan, H., Aravind, U.K., Aravindakumar, C.T. Free Radic. Biol. Med. (2006) [Pubmed]
  4. Mass spectrometric interrogation of thioester-bound intermediates in the initial stages of epothilone biosynthesis. Hicks, L.M., O'Connor, S.E., Mazur, M.T., Walsh, C.T., Kelleher, N.L. Chem. Biol. (2004) [Pubmed]
  5. Demonstration of the catalytic roles and evidence for the physical association of type I fatty acid synthases and a polyketide synthase in the biosynthesis of aflatoxin B1. Watanabe, C.M., Wilson, D., Linz, J.E., Townsend, C.A. Chem. Biol. (1996) [Pubmed]
  6. The development and application of a novel chromophoric substrate for investigation of the mechanism of yeast fatty acid synthase. Singh, N., Wakil, S.J., Stoops, J.K. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  7. Kinetics and mechanism of the addition of nucleophiles to alpha,beta-unsaturated thiol esters. Hartman, R.F., Rose, S.D. J. Org. Chem. (2006) [Pubmed]
  8. Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases. Liou, G.F., Lau, J., Cane, D.E., Khosla, C. Biochemistry (2003) [Pubmed]
  9. High-throughput mutagenesis to evaluate models of stereochemical control in ketoreductase domains from the erythromycin polyketide synthase. O'Hare, H.M., Baerga-Ortiz, A., Popovic, B., Spencer, J.B., Leadlay, P.F. Chem. Biol. (2006) [Pubmed]
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