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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Sep;78(9):5440–5444. doi: 10.1073/pnas.78.9.5440

Chemical synthesis of acyl thioesters of acyl carrier protein with native structure.

J E Cronan Jr, A L Klages
PMCID: PMC348761  PMID: 7029535

Abstract

The acyl carrier protein (ACP) of Escherichia coli was converted to acyl-ACP by imidazole-catalyzed S-acylation with N-acylimidazole. The acylation was specific to the sulfhydryl group; no acylation of tyrosine or amino groups of the protein occurred. The acyl-ACP substrates synthesized had a native structure as determined by gel electrophoresis, hydrophobic chromatography, and enzymatic activity. N-Acylimidazoles are readily synthesized and permit preparation of those acyl-ACP substrates that cannot be produced enzymatically.

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Selected References

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