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

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Title: High Production of Ergothioneine in Escherichia coli using the Sulfoxide Synthase from Methylobacterium strains
Authors: Kamide, Tomoyuki Browse this author
Takusagawa, Shun Browse this author
Tanaka, Naoyuki Browse this author
Ogasawara, Yasushi Browse this author
Kawano, Yusuke Browse this author
Ohtsu, Iwao Browse this author
Satoh, Yasuharu Browse this author →KAKEN DB
Dairi, Tohru Browse this author →KAKEN DB
Keywords: ergothioneine
heterologous production
Escherichia coli
Issue Date: 10-Jun-2020
Publisher: American Chemical Society
Journal Title: Journal of Agricultural and Food Chemistry
Volume: 68
Issue: 23
Start Page: 6390
End Page: 6394
Publisher DOI: 10.1021/acs.jafc.0c01846
Abstract: 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 gamma-glutamylcysteine (gamma GC) to HER to yield hercynyl-gamma-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 gamma GC. We reconstituted the ERG production system in E. coli with egtB from M. pseudosasicola; ERG productivity reached 657 mg L-1.
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Agricultural and Food Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see, see
Type: article (author version)
Appears in Collections:工学院・工学研究院 (Graduate School of Engineering / Faculty of Engineering) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 佐藤 康治

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