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

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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 SH 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.