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Mapping enzyme catalysis with metabolic biosensing

Author

Listed:
  • Linfeng Xu

    (University of California, San Francisco)

  • Kai-Chun Chang

    (University of California, San Francisco)

  • Emory M. Payne

    (University of Michigan)

  • Cyrus Modavi

    (University of California, San Francisco)

  • Leqian Liu

    (University of California, San Francisco)

  • Claire M. Palmer

    (The University of Texas at Austin)

  • Nannan Tao

    (Bruker Nano Surfaces)

  • Hal S. Alper

    (The University of Texas at Austin
    The University of Texas at Austin)

  • Robert T. Kennedy

    (University of Michigan)

  • Dale S. Cornett

    (Bruker Daltonics)

  • Adam R. Abate

    (University of California, San Francisco
    Chan Zuckerberg Biohub)

Abstract

Enzymes are represented across a vast space of protein sequences and structural forms and have activities that far exceed the best chemical catalysts; however, engineering them to have novel or enhanced activity is limited by technologies for sensing product formation. Here, we describe a general and scalable approach for characterizing enzyme activity that uses the metabolism of the host cell as a biosensor by which to infer product formation. Since different products consume different molecules in their synthesis, they perturb host metabolism in unique ways that can be measured by mass spectrometry. This provides a general way by which to sense product formation, to discover unexpected products and map the effects of mutagenesis.

Suggested Citation

  • Linfeng Xu & Kai-Chun Chang & Emory M. Payne & Cyrus Modavi & Leqian Liu & Claire M. Palmer & Nannan Tao & Hal S. Alper & Robert T. Kennedy & Dale S. Cornett & Adam R. Abate, 2021. "Mapping enzyme catalysis with metabolic biosensing," Nature Communications, Nature, vol. 12(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27185-9
    DOI: 10.1038/s41467-021-27185-9
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    Cited by:

    1. Allwin D. McDonald & Peyton M. Higgins & Andrew R. Buller, 2022. "Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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