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- W3026189910 abstract "Abstract Enzyme assemblies such as type II polyketide synthases (PKSs) produce a wide array of bioactive secondary metabolites. While the molecules produced by type II PKSs have found remarkable success in the clinic, the biosynthetic prowess of these enzymes has been stymied by: 1) the inability to reconstitute the bioactivity of the minimal PKS enzymes in vitro and 2) limited exploration of type II PKSs from diverse phyla. Towards filling this unmet need, we expressed, purified, and characterized the ketosynthase chain length factor (KSCLF) and acyl carrier protein (ACP) from Ktedonobacter racemifer . Using E. coli as a heterologous host, we obtained soluble proteins in titers representing significant improvements over previous KSCLF heterologous expression efforts. Characterization of these enzymes reveals that Kr ACP has self-malonylating activity. Sedimentation velocity analytical ultracentrifugation (SV-AUC) analysis of holo - Kr ACP and Kr KSCLF indicates that these enzymes do not interact in vitro , suggesting that the acylated state of these proteins might play an important role in facilitating biosynthetically relevant interactions. Given the potential impact of obtaining soluble core type II PKS biosynthetic enzymes to enable in vitro characterization studies, these results lay important groundwork for optimizing the interaction between Kr KSCLF and Kr ACP and exploring the biosynthetic potential of other non-actinomycete type II PKSs." @default.
- W3026189910 created "2020-05-29" @default.
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- W3026189910 date "2020-05-21" @default.
- W3026189910 modified "2023-10-14" @default.
- W3026189910 title "Widening the bottleneck: Heterologous expression, purification, and characterization of the Ktedonobacter racemifer minimal type II polyketide synthase in Escherichia coli" @default.
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- W3026189910 doi "https://doi.org/10.1101/2020.05.18.102780" @default.
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