Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes.
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.
Institut National de la Recherche Agronomique, UMR 1319 Micalis, Jouy-en-Josas, France.
Stéphane
S
Pierre
Alain
A
Guillot
Alhosna
A
Benjdia
Corine
C
Sandström
Philippe
P
Langella
Olivier
O
Berteau
D003001:Cloning, Molecular; D004227:Dithionite / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism; D008780:Methyltransferases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012436:S-Adenosylmethionine / Q000378:metabolism* / Q000494:pharmacology; D013056:Spectrophotometry, Ultraviolet; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013883:Thiostrepton / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism; D014805:Vitamin B 12 / Q000031:analogs & derivatives / Q000378:metabolism
D011994:Recombinant Proteins; D013439:Sulfhydryl Reagents; D004227:Dithionite; D012436:S-Adenosylmethionine; D014364:Tryptophan; C019476:mecobalamin; D008780:Methyltransferases; C063542:tryptophan 2-methyltransferase; D013883:Thiostrepton; D014805:Vitamin B 12; D004229:Dithiothreitol