Journal
CHEMBIOCHEM
Volume 21, Issue 20, Pages 2908-2911Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000232
Keywords
ergothioneine; methyltransferase; Mycobacterium tuberculosis; protein kinase; regulation
Funding
- Swiss National Science Foundation
- University of Basel
- Professur fur Molekulare Bionik
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Ergothioneine has emerged as a crucial cytoprotectant in the pathogenic lifestyle ofMycobacterium tuberculosis. Production of this antioxidant from primary metabolites may be regulated by phosphorylation of Thr213 in the active site of the methyltransferase EgtD. The structure of mycobacterial EgtD suggests that this post-translational modification would require a large-scale change in conformation to make the active-site residue accessible to a protein kinase. In this report, we show that, underin vitroconditions, EgtD is not a substrate of protein kinase PknD.
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