Work

Priming Type II Polyketide Synthases via a Type II Nonribosomal Peptide Synthetase Mechanism

Year: 2006

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja0559707

Authors: Miho Izumikawa, Qian Cheng, Bradley S. Moore

Institutions: University of Arizona, Scripps Institution of Oceanography, University of California San Diego

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Applied Microbiology and Biotechnology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of Allergy and Infectious Diseases

Awards: Biosynthesis of Marine Polyketide Antibiotics, G1745768855, Biosynthesis of Marine Polyketide Antibiotics