論文

査読有り 国際誌
2020年6月10日

High Production of Ergothioneine in Escherichia coli using the Sulfoxide Synthase from Methylobacterium strains.

Journal of agricultural and food chemistry
  • Tomoyuki Kamide
  • ,
  • Shun Takusagawa
  • ,
  • Naoyuki Tanaka
  • ,
  • Yasushi Ogasawara
  • ,
  • Yusuke Kawano
  • ,
  • Iwao Ohtsu
  • ,
  • Yasuharu Satoh
  • ,
  • Tohru Dairi

68
23
開始ページ
6390
終了ページ
6394
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/acs.jafc.0c01846

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.

リンク情報
DOI
https://doi.org/10.1021/acs.jafc.0c01846
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32436380

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