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Clicking into Place: Interfacing Terminal Alkyne Biosynthesis with Polyketide Synthases

https://doi.org/10.1016/j.tibtech.2020.04.001Get rights and content

Engineering polyketide biosynthesis to enable the production of diverse chemical structures is a major challenge at present. Utilising an established biosynthetic cassette for terminal alkyne production, Porterfield et al. applied docking domain and site-directed mutagenesis approaches to interface these enzymes with modular polyketide synthase (PKS) enzymes, yielding products with a bio-orthogonal handle.

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  • Probing the structure and function of acyl carrier proteins to unlock the strategic redesign of type II polyketide biosynthetic pathways

    2021, Journal of Biological Chemistry
    Citation Excerpt :

    Harnessing the terminal alkyne biosynthetic machinery from the jamaicamide B type I PKS pathway enabled access to in trans loading of alkyne polyketides onto noncognate type I PKS enzymes. This process was optimized through the strategic modification of the jamaicamide B ACP via docking domain installation and site-directed mutagenesis (107, 108). The selective, copper-catalyzed reaction of the terminal alkyne with an azide-containing fluorophore or mass tag can potentially enable subsequent visualization via fluorescence or mass spectrometry.

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