Reexamination of the Ergothioneine Biosynthetic Methyltransferase EgtD from Mycobacterium tuberculosis as a Protein Kinase Substrate

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Reexamination of the Ergothioneine Biosynthetic Methyltransferase EgtD from Mycobacterium tuberculosis as a Protein Kinase Substrate

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4614550
Author(s)	Maurer, Alice; Seebeck, Florian P.
Author(s) at UniBasel	Seebeck, Florian Peter Maurer, Alice
Year	2020
Title	Reexamination of the Ergothioneine Biosynthetic Methyltransferase EgtD from Mycobacterium tuberculosis as a Protein Kinase Substrate
Journal	ChemBioChem
Volume	21
Number	20
Pages / Article-Number	2908-2911
Keywords	Mycobacterium tuberculosis; ergothioneine; methyltransferase; protein kinase; regulation
Abstract	Ergothioneine has emerged as a crucial cytoprotectant in the pathogenic lifestyle of Mycobacterium 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, under in vitro conditions, EgtD is not a substrate of protein kinase PknD.
Publisher	Wiley
ISSN/ISBN	1439-4227 ; 1439-7633
edoc-URL	https://edoc.unibas.ch/81362/
Full Text on edoc	No
Digital Object Identifier DOI	10.1002/cbic.202000232
PubMed ID	http://www.ncbi.nlm.nih.gov/pubmed/32614492
Document type (ISI)	Journal Article

11/05/2024

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