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Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC

Vit, Allegra and Mashabela, Gabriel and Blankenfeldt, Wulf and Seebeck, Florian P.. (2015) Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. ChemBioChem, 16 (10). pp. 1490-1496.

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Official URL: http://edoc.unibas.ch/41780/

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Abstract

The ubiquitous sulfur metabolite ergothioneine is biosynthesized by oxidative attachment of a sulfur atom to the imidazole ring of Nα-trimethylhistidine. Most actinobacteria, including Mycobacterium tuberculosis, use γ-glutamyl cysteine as a sulfur donor. In subsequent steps the carbon scaffold of γ-glutamyl cysteine is removed by the glutamine amidohydrolase EgtC and the β-lyase EgtE. We determined the crystal structure of EgtC from Mycobacterium smegmatis in complex with its physiological substrate. The set of active site residues that define substrate specificity in EgtC are highly conserved, even in homologues that are not involved in ergothioneine production. This conservation is compounded by the phylogenetic distribution of EgtC-like enzymes indicates that their last common ancestor might have emerged for a purpose other than ergothioneine production.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Molecular Bionics (Seebeck)
UniBasel Contributors:Seebeck, Florian Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:1439-4227
e-ISSN:1439-7633
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:12 Apr 2017 09:29
Deposited On:25 Apr 2016 13:26

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