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Aminoacyl chain translocation catalysed by a type II thioesterase domain in an unusual non-ribosomal peptide synthetase

Author

Listed:
  • Shan Wang

    (University of Aberdeen)

  • William D. G. Brittain

    (Durham University, Science Site)

  • Qian Zhang

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery (MOE) and Hubei Province Engineering and Technology Research Centre for Fluorinated Pharmaceuticals, School of Pharmaceutical Sciences, Wuhan University)

  • Zhou Lu

    (University of Aberdeen)

  • Ming Him Tong

    (University of Aberdeen)

  • Kewen Wu

    (University of Aberdeen)

  • Kwaku Kyeremeh

    (University of Ghana)

  • Matthew Jenner

    (University of Warwick
    University of Warwick)

  • Yi Yu

    (Key Laboratory of Combinatorial Biosynthesis and Drug Discovery (MOE) and Hubei Province Engineering and Technology Research Centre for Fluorinated Pharmaceuticals, School of Pharmaceutical Sciences, Wuhan University)

  • Steven L. Cobb

    (Durham University, Science Site)

  • Hai Deng

    (University of Aberdeen)

Abstract

Non-Ribosomal Peptide Synthetases (NRPSs) assemble a diverse range of natural products with important applications in both medicine and agriculture. They consist of several multienzyme subunits that must interact with each other in a highly controlled manner to facilitate efficient chain transfer, thus ensuring biosynthetic fidelity. Several mechanisms for chain transfer are known for NRPSs, promoting structural diversity. Herein, we report the first biochemically characterized example of a type II thioesterase (TEII) domain capable of catalysing aminoacyl chain transfer between thiolation (T) domains on two separate NRPS subunits responsible for installation of a dehydrobutyrine moiety. Biochemical dissection of this process reveals the central role of the TEII-catalysed chain translocation event and expands the enzymatic scope of TEII domains beyond canonical (amino)acyl chain hydrolysis. The apparent co-evolution of the TEII domain with the NRPS subunits highlights a unique feature of this enzymatic cassette, which will undoubtedly find utility in biosynthetic engineering efforts.

Suggested Citation

  • Shan Wang & William D. G. Brittain & Qian Zhang & Zhou Lu & Ming Him Tong & Kewen Wu & Kwaku Kyeremeh & Matthew Jenner & Yi Yu & Steven L. Cobb & Hai Deng, 2022. "Aminoacyl chain translocation catalysed by a type II thioesterase domain in an unusual non-ribosomal peptide synthetase," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-021-27512-0
    DOI: 10.1038/s41467-021-27512-0
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    References listed on IDEAS

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    1. Frédéric H. Vaillancourt & Ellen Yeh & David A. Vosburg & Sarah E. O'Connor & Christopher T. Walsh, 2005. "Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis," Nature, Nature, vol. 436(7054), pages 1191-1194, August.
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