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Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4508204
Author(s) Leisinger, Florian; Burn, Reto; Meury, Marcel; Lukat, Peer; Seebeck, Florian P.
Author(s) at UniBasel Seebeck, Florian Peter
Year 2019
Title Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis
Journal Journal of the American Chemical Society
Volume 141
Number 17
Pages / Article-Number 6906-6914
Mesh terms Science & TechnologyPhysical SciencesChemistry, MultidisciplinaryChemistry
Abstract Ergothioneine is an emergent factor in cellular redox biochemistry in humans and pathogenic bacteria. Broad consensus has formed around the idea that ergothioneine protects cells against reactive oxygen species. The recent discovery that anaerobic microorganisms make the same metabolite using oxygen-independent chemistry indicates that ergothioneine also plays physiological roles under anoxic conditions. In this report, we describe the crystal structure of the anaerobic ergothioneine biosynthetic enzyme EanB from green sulfur bacterium Chlorobium limicola. This enzyme catalyzes the oxidative sulfurization of N-alpha-trimethyl histidine. On the basis of structural and kinetic evidence, we describe the catalytic mechanism of this unusual C-S bond-forming reaction. Significant active-site conservation among distant EanB homologues suggests that the oxidative sulfurization of heterocyclic substrates may occur in a broad range of bacteria.
Publisher American Chemical Society
ISSN/ISBN 0002-7863 ; 1520-5126
edoc-URL https://edoc.unibas.ch/75085/
Full Text on edoc Available
Digital Object Identifier DOI 10.1021/jacs.8b12596
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/30943021
ISI-Number 000466987900021
Document type (ISI) Journal Article
 
   

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