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Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Agric. Food Chem. 2020, 68, 23, 6390-6394
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High Production of Ergothioneine in Escherichia coli using the Sulfoxide Synthase from Methylobacterium strains

  • Tomoyuki Kamide
    Tomoyuki Kamide
    Graduate School of Chemical Science and Engineering, Hokkaido University, N13-W8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan
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    • , 
  • Shun Takusagawa
    Shun Takusagawa
    Graduate School of Chemical Science and Engineering, Hokkaido University, N13-W8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan
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    • , 
  • Naoyuki Tanaka
    Naoyuki Tanaka
    Faculty of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan
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    • , 
  • Yasushi Ogasawara
    Yasushi Ogasawara
    Graduate School of Engineering, Hokkaido University, N13-W8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan
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    Orcidhttp://orcid.org/0000-0002-3144-3985
    • , 
  • Yusuke Kawano
    Yusuke Kawano
    Faculty of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan
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    • , 
  • Iwao Ohtsu
    Iwao Ohtsu
    Faculty of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan
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    • , 
  • Yasuharu Satoh*
    Yasuharu Satoh
    Graduate School of Engineering, Hokkaido University, N13-W8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan
    *Email: [email protected]. Phone: +81-11-706-7818; Fax: +81-11-706-7818.
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    Orcidhttp://orcid.org/0000-0001-6671-7758
    • , and 
  • Tohru Dairi*
    Tohru Dairi
    Graduate School of Engineering, Hokkaido University, N13-W8, Kita-ku, Sapporo, Hokkaido 060-8628, Japan
    *Email: [email protected]. Phone: +81-11-706-7815; Fax: +81-11-706-7118.
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    Orcidhttp://orcid.org/0000-0002-3406-7970
Cite this: J. Agric. Food Chem. 2020, 68, 23, 6390–6394
Publication Date (Web):May 21, 2020
https://doi.org/10.1021/acs.jafc.0c01846
Copyright © 2020 American Chemical Society
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Abstract

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We previously constructed a heterologous production system for ergothioneine (ERG) in Escherichia coli using five ERG biosynthesis genes (egtABCDE) from Mycobacterium smegmatis. However, significant amounts of hercynine (HER), an intermediate of ERG, as ERG were accumulated, suggesting that the reaction of EgtB catalyzing the attachment of γ-glutamylcysteine (γGC) to HER to yield hercynyl-γ-glutamylcysteine sulfoxide was a bottleneck. In this study, we searched for other EgtBs and found many egtB orthologs in diverse microorganisms. Among these, Methylobacterium strains possessed EgtBs that catalyze the direct conversion of HER into hercynylcysteine sulfoxide with l-cysteine (l-Cys) as a sulfur donor, in a manner similar to those of acidobacterial CthEgtB and fungal Egt1. An in vitro study with recombinant EgtBs from Methylobacterium brachiatum and Methylobacterium pseudosasicola clearly showed that both enzymes accepted l-Cys but not γGC. We reconstituted the ERG production system in E. coli with egtB from M. pseudosasicola; ERG productivity reached 657 mg L–1.

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The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.jafc.0c01846.

  • Sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of Mb_EgtB and Mp_EgtB production (Figure S1); mass spectra of in vitro reaction products of l-Cys and recombinant EgtBs from M. brachiatum and M. pseudosasicola (Figure S2); comparison of various EgtB activities (Figure S3); effect of pH and temperature on Mp_EgtB activity (Figure S4); Michaelis–Menten plots of the Mp_EgtB for HER and l-Cys (Figure S5); Michaelis–Menten plots of the Mb_EgtB for HER and l-Cys (Figure S6); 1H NMR spectrum of HER (Figure S7); 13C NMR spectrum of HER (Figure S8); identities of amino acid sequences of type I–V EgtBs (Table S1); and primers used in this study (Table S2) (PDF)

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Cited By

This article is cited by 2 publications.

  1. Yiwen Han, Xiuyang Tang, Yuting Zhang, Xuechao Hu, Lu-Jing Ren. The current status of biotechnological production and the application of a novel antioxidant ergothioneine. Critical Reviews in Biotechnology 2021, 149 , 1-26. https://doi.org/10.1080/07388551.2020.1869692
  2. Irwin K. Cheah, Barry Halliwell. Ergothioneine, recent developments. Redox Biology 2021, 37 , 101868. https://doi.org/10.1016/j.redox.2021.101868

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