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Chemical Compound Review:

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

Synonyms: ACMC-20ak7f, CHEBI:74410, CPD-10671, NSC-38835, LS-9810, ...

Baerga-Ortiz, A. et al., Manoj, V.M. et al., Singh, N. et al., Hicks, L.M. et al., Yin, Y. et al., et al.

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High impact information on N-Acetyl cysteamin

The substrate specificity of PICS modules 5+TE and 6+TE was investigated using N-acetylcysteamine thioesters of 2-methyl-3-hydroxy-pentanoic acid as diketide analogues of the natural polyketide chain elongation substrates [1].
Modeling of eryKR(1) and eryKR(2) showed that conserved amino acids previously correlated with production of alternative alcohol configurations lie in the active site. eryKR(1) domains mutated at these positions showed an altered stereochemical outcome in reduction of (2R, S)-2-methyl-3-oxopentanoic acid N-acetylcysteamine thioester [2].
Both kinetics of the reaction and the mechanistic aspects of the decomposition of S-nitroso derivatives of glutathione, L-cysteine, N-acetyl-L-cysteine, N-acetyl-D,L-penicillamine, N-acetylcysteamine, L-cysteine methyl ester, and D,L-penicillamine have been investigated at neutral and acidic pH [3].
Incubation with various N-acetylcysteamine thioester (S-NAC) substrate mimics produced mass shifts on the EpoC ACP domain consistent with their condensation with an enzyme-bound carbanion produced by the decarboxylation of methylmalonyl-S-EpoC [4].
RESULTS: The N-acetylcysteamine (NAC) thioester of hexanoic acid was shown to efficiently support the biosynthesis of norsolorinic acid (compound 3. ) in the NOR-1 strain [5].

Biological context of N-Acetyl cysteamin

A probable kinetic scheme for enzyme catalyzed transacetylation from p-nitrophenylthiol acetate to an acyl acceptor (CoA or N-acetylcysteamine) is proposed and the kinetic constants for acetylation of enzyme and for acetyl transfer to an acceptor were determined [6].

Associations of N-Acetyl cysteamin with other chemical compounds

The kinetics of the reactions of these thiol esters with N-acetyl-l-cysteine (NAC), N-acetylcysteamine, and N(2)-acetyl-L-lysine (NAL) have been studied, and the thiol addition products have been identified [7].

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].

References

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]
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]
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]
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]
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]
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]
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]
Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases. Liou, G.F., Lau, J., Cane, D.E., Khosla, C. Biochemistry (2003) [Pubmed]
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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