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Journal Article

Understanding Substrate Selectivity of Phoslactomycin Polyketide Synthase by Using Reconstituted in Vitro Systems

MPS-Authors
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Geyer,  Kyra
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Sundaram,  Srividhya
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Erb,  Tobias J.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Geyer, K., Sundaram, S., Susnik, P., Koert, U., & Erb, T. J. (2020). Understanding Substrate Selectivity of Phoslactomycin Polyketide Synthase by Using Reconstituted in Vitro Systems. CHEMBIOCHEM, 21(14), 2080-2085. doi:10.1002/cbic.202000112.


Cite as: https://hdl.handle.net/21.11116/0000-0008-BE98-7
Abstract
Polyketide synthases (PKSs) use simple extender units to synthesize
complex natural products. A fundamental question is how different
extender units are site-specifically incorporated into the growing
polyketide. Here we established phoslactomycin (Pn) PKS, which
incorporates malonyl- and ethylmalonyl-CoA, as an in vitro model to
study substrate specificity. We combined up to six Pn PKS modules with
different termination sites for the controlled release of tetra-, penta-
and hexaketides, and challenged these systems with up to seven different
extender units in competitive assays to test for the specificity of Pn
modules. While malonyl-CoA modules of Pn PKS exclusively accept their
natural substrate, the ethylmalonyl-CoA module PnC tolerates different
alpha-substituted derivatives, but discriminates against malonyl-CoA. We
show that the ratio of extender transacylation to hydrolysis controls
incorporation in PnC, thus explaining site-specific selectivity and
promiscuity in the natural context of Pn PKS.