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Updated: Jul 13, 2026

High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles
Published on: July 6, 2012
Priming type II polyketide synthases via a type II nonribosomal peptide synthetase mechanism
Miho Izumikawa1, Qian Cheng, Bradley S Moore
1College of Pharmacy, University of Arizona, Tucson, Arizona 85721, USA.
Abstract:
Benzoic acid priming of the enterocin and actinorhodin type II polyketide synthase complexes was accomplished in vitro via an unprecedented type II nonribosomal peptide synthetase-like mechanism involving the benzoate:acyl carrier protein (ACP) ligase EncN and the ACP EncC. The transfer of the aryl acid to the ACP is ATP-dependent, yet coenzyme A-independent, as characterized with radiolabeled substrates and protein mass spectrometry. Subsequent transport of the ACP-bound aryl group to the native enterocin and the aberrant actinorhodin ketosynthase chain length factor heterodimers was further demonstrated, thereby demonstrating the potential of this biocatalyst for engineering diverse aryl-primed aromatic polyketide agents.
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