Journal Article

PUBDB-2015-02411

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC

Vit, A. ; Mashabela, G. T. ; Blankenfeldt, W. ; Seebeck, F. P. (Corresponding author)

2015
Wiley-VCH Weinheim

This record in other databases:        

Please use a persistent id in citations: doi:10.1002/cbic.201500168

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.

Note: (c) WILEY-VCH Verlag GmbH & Co. KGaA. Post referee full text in progress. Embargo for fill text 1 year from 16 JUN 2015.

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Contributing Institute(s):

1. DOOR-User (DOOR)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)

Experiment(s):

1. PETRA Beamline P11 (PETRA III)

Appears in the scientific report 2015

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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