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Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis

The Journal of Antibiotics volume 78, pages 639–650 (2025)Cite this article

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Abstract

α/β hydrolase fold thioesterases (TEs) play fundamentally important roles in polyketide and non-ribosomal peptide biosynthesis. Type-I TEs, fused at the C-terminus of multi-modular enzymatic assembly lines, dictate the overall molecular shapes of assembly-line products, while standalone type-II TEs maintain assembly-line activity through proofreading functions. Beyond these established roles, recent studies have elucidated several distinct TE functions that expand the functional versatility of these enzymes. This review summarizes recently discovered non-canonical functions of TEs in bacterial non-ribosomal peptide biosynthesis.

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Acknowledgements

I gratefully acknowledge Prof. Toshiyuki Wakimoto (Hokkaido University) and colleagues for their support of this work. This work was partly supported by Hokkaido University, Global Facility Center (GFC), Pharma Science Open Unit (PSOU), funded by the Ministry of Education, Culture, Sports, Science and Technology (MEXT) under “Support Program for Implementation of New Equipment Sharing System”, Global Station for Biosurfaces and Drug Discovery, a project of Global Institution for Collaborative Research and Education in Hokkaido University, the Japan Agency for Medical Research and Development JP25gm1610007, the Japan Science and Technology Agency(JST Grant Number ACT-X JPMJAX201F, FOREST JPMJFR233U), and JSPS KAKENHI (Grant Numbers JP23K17410, JP24K01659).

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  1. Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan

    Kenichi Matsuda

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Matsuda, K. Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis. J Antibiot 78, 639–650 (2025). https://doi.org/10.1038/s41429-025-00854-3

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