Metabolic pathway assembly using docking domains from type I cis-AT polyketide synthases

Xixi Sun, Yujie Yuan, Qitong Chen, Shiqi Nie, Jiaxuan Guo, Zutian Ou, Min Huang, Zixin Deng (), Tiangang Liu () and Tian Ma ()
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Xixi Sun: Chinese Academy of Sciences
Yujie Yuan: Chinese Academy of Sciences
Qitong Chen: Chinese Academy of Sciences
Shiqi Nie: Chinese Academy of Sciences
Jiaxuan Guo: Chinese Academy of Sciences
Zutian Ou: Chinese Academy of Sciences
Min Huang: Chinese Academy of Sciences
Zixin Deng: Wuhan University
Tiangang Liu: Wuhan University
Tian Ma: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Engineered metabolic pathways in microbial cell factories often have no natural organization and have challenging flux imbalances, leading to low biocatalytic efficiency. Modular polyketide synthases (PKSs) are multienzyme complexes that synthesize polyketide products via an assembly line thiotemplate mechanism. Here, we develop a strategy named mimic PKS enzyme assembly line (mPKSeal) that assembles key cascade enzymes to enhance biocatalytic efficiency and increase target production by recruiting cascade enzymes tagged with docking domains from type I cis-AT PKS. We apply this strategy to the astaxanthin biosynthetic pathway in engineered Escherichia coli for multienzyme assembly to increase astaxanthin production by 2.4-fold. The docking pairs, from the same PKSs or those from different cis-AT PKSs evidently belonging to distinct classes, are effective enzyme assembly tools for increasing astaxanthin production. This study addresses the challenge of cascade catalytic efficiency and highlights the potential for engineering enzyme assembly.

Date: 2022
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DOI: 10.1038/s41467-022-33272-2

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