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• W2021104514 endingPage "15421" @default.
• W2021104514 startingPage "15414" @default.
• W2021104514 abstract "During polyketide biosynthesis, malonyl groups are transferred to the acyl carrier protein (ACP) component of the polyketide synthase (PKS), and it has been shown that a number of type II polyketide ACPs undergo rapid self-acylation from malonyl-CoA in the absence of a malonyl-CoA:holo-acyl carrier protein transacylase (MCAT). More recently, however, the observation of self-malonylation has been ascribed to contamination with Escherichia coli MCAT (FabD) rather than an intrinsic property of the ACP. The wild-type apo-ACP from the actinorhodin (act) PKS of Streptomyces coelicolor (synthetic apo-ACP) has therefore been synthesized using solid-state peptide methods and refolded using the GroEL/ES chaperone system from E. coli. Correct folding of the act ACP has been confirmed by circular dichroism (CD) and 1H NMR. Synthetic apo-ACP was phosphopantetheinylated to 100% by S. coelicolor holo-acyl carrier protein synthase (ACPS), and the resultant holo-ACP underwent self-malonylation in the presence of malonyl-CoA. No malonylation of negative controls was observed, confirming that the use of ACPS and GroEL/ES did not introduce contamination with E. coli MCAT. This result proves unequivocally that self-malonylation is an inherent activity of this PKS ACP in vitro." @default.
• W2021104514 created "2016-06-24" @default.
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• W2021104514 date "2005-10-26" @default.
• W2021104514 modified "2023-10-10" @default.
• W2021104514 title "Self-Malonylation Is an Intrinsic Property of a Chemically Synthesized Type II Polyketide Synthase Acyl Carrier Protein^," @default.
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• W2021104514 doi "https://doi.org/10.1021/bi051499i" @default.
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