Abstract
Methylation is among the most widespread chemical modifications encountered in biomolecules and has a pivotal role in many major biological processes. In the biosynthetic pathway of the antibiotic thiostrepton A, we identified what is to our knowledge the first tryptophan methyltransferase. We show that it uses unprecedented chemistry to methylate inactivated sp(2)-hybridized carbon atoms, despite being predicted to be a radical SAM enzyme.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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Dithionite / pharmacology
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Dithiothreitol / pharmacology
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Escherichia coli / metabolism
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Methyltransferases / metabolism*
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Recombinant Proteins / biosynthesis
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S-Adenosylmethionine / metabolism*
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S-Adenosylmethionine / pharmacology
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Spectrophotometry, Ultraviolet
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Sulfhydryl Reagents / pharmacology
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Thiostrepton / metabolism*
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Tryptophan / metabolism
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Vitamin B 12 / analogs & derivatives
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Vitamin B 12 / metabolism
Substances
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Recombinant Proteins
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Sulfhydryl Reagents
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Dithionite
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S-Adenosylmethionine
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Tryptophan
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mecobalamin
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Methyltransferases
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tryptophan 2-methyltransferase
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Thiostrepton
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Vitamin B 12
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Dithiothreitol