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Modular enzyme assembly for enhanced cascade biocatalysis and metabolic flux

Author

Listed:
  • Wei Kang

    (The Chinese University of Hong Kong)

  • Tian Ma

    (Wuhan University)

  • Min Liu

    (The Chinese University of Hong Kong)

  • Jiale Qu

    (The Chinese University of Hong Kong)

  • Zhenjun Liu

    (The Chinese University of Hong Kong)

  • Huawei Zhang

    (The Chinese University of Hong Kong)

  • Bin Shi

    (Wuhan University)

  • Shuai Fu

    (J1 Biotech Co., Ltd.)

  • Juncai Ma

    (The Chinese University of Hong Kong)

  • Louis Tung Faat Lai

    (The Chinese University of Hong Kong)

  • Sicong He

    (Hong Kong University of Science and Technology)

  • Jianan Qu

    (Hong Kong University of Science and Technology)

  • Shannon Wing-Ngor Au

    (The Chinese University of Hong Kong)

  • Byung Ho Kang

    (The Chinese University of Hong Kong)

  • Wilson Chun Yu Lau

    (The Chinese University of Hong Kong)

  • Zixin Deng

    (Wuhan University
    Shanghai Jiao Tong University)

  • Jiang Xia

    (The Chinese University of Hong Kong)

  • Tiangang Liu

    (Wuhan University)

Abstract

Enzymatic reactions in living cells are highly dynamic but simultaneously tightly regulated. Enzyme engineers seek to construct multienzyme complexes to prevent intermediate diffusion, to improve product yield, and to control the flux of metabolites. Here we choose a pair of short peptide tags (RIAD and RIDD) to create scaffold-free enzyme assemblies to achieve these goals. In vitro, assembling enzymes in the menaquinone biosynthetic pathway through RIAD–RIDD interaction yields protein nanoparticles with varying stoichiometries, sizes, geometries, and catalytic efficiency. In Escherichia coli, assembling the last enzyme of the upstream mevalonate pathway with the first enzyme of the downstream carotenoid pathway leads to the formation of a pathway node, which increases carotenoid production by 5.7 folds. The same strategy results in a 58% increase in lycopene production in engineered Saccharomyces cerevisiae. This work presents a simple strategy to impose metabolic control in biosynthetic microbe factories.

Suggested Citation

  • Wei Kang & Tian Ma & Min Liu & Jiale Qu & Zhenjun Liu & Huawei Zhang & Bin Shi & Shuai Fu & Juncai Ma & Louis Tung Faat Lai & Sicong He & Jianan Qu & Shannon Wing-Ngor Au & Byung Ho Kang & Wilson Chun, 2019. "Modular enzyme assembly for enhanced cascade biocatalysis and metabolic flux," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12247-w
    DOI: 10.1038/s41467-019-12247-w
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    Cited by:

    1. Wenwen Yu & Ke Jin & Dandan Wang & Nankai Wang & Yangyang Li & Yanfeng Liu & Jianghua Li & Guocheng Du & Xueqin Lv & Jian Chen & Rodrigo Ledesma-Amaro & Long Liu, 2024. "De novo engineering of programmable and multi-functional biomolecular condensates for controlled biosynthesis," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Yameng Xu & Xinglong Wang & Chenyang Zhang & Xuan Zhou & Xianhao Xu & Luyao Han & Xueqin Lv & Yanfeng Liu & Song Liu & Jianghua Li & Guocheng Du & Jian Chen & Rodrigo Ledesma-Amaro & Long Liu, 2022. "De novo biosynthesis of rubusoside and rebaudiosides in engineered yeasts," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Xixi Sun & Yujie Yuan & Qitong Chen & Shiqi Nie & Jiaxuan Guo & Zutian Ou & Min Huang & Zixin Deng & Tiangang Liu & Tian Ma, 2022. "Metabolic pathway assembly using docking domains from type I cis-AT polyketide synthases," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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