Chemical synthesis of acyl thioesters of acyl carrier protein with native structure.
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.
D000213:Acyl Carrier Protein / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D004952:Esters / Q000138:chemical synthesis; D007700:Kinetics; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds
D000213:Acyl Carrier Protein; D004952:Esters; D013438:Sulfhydryl Compounds