Priming type II polyketide synthases via a type II nonribosomal peptide synthetase mechanism |
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Authors: | Izumikawa Miho Cheng Qian Moore Bradley S |
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Affiliation: | College of Pharmacy, University of Arizona, Tucson, Arizona 85721, USA. |
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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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