Journal
CHEMICAL COMMUNICATIONS
Volume 56, Issue 14, Pages 2115-2118Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9cc07807j
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Funding
- ERC [772280]
- DFG [SFB858, IRTG 2027]
- NIAID, NIH [HHSN272201700059C]
- HHS [HHSN272201700059C]
- European Research Council (ERC) [772280] Funding Source: European Research Council (ERC)
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Methyltransferases (MTases) modify a wide range of biomolecules using S-adenosyl-l-methionine (AdoMet) as the cosubstrate. Synthetic AdoMet analogues are powerful tools to site-specifically introduce a variety of functional groups and exhibit potential to be converted only by distinct MTases. Extending the size of the substituent at the sulfur/selenium atom provides selectivity among MTases but is insufficient to discriminate between promiscuous MTases. We present a panel of AdoMet analogues differing in the nucleoside moiety (NM-AdoMets). These NM-AdoMets were efficiently produced by a previously uncharacterized methionine adenosyltransferase (MAT) from methionine and ATP analogues, such as ITP and N-6-propargyl-ATP. The N-6-modification changed the relative activity of three representative MTases up to 13-fold resulting in discrimination of substrates for the methyl transfer and could also be combined with transfer of allyl and propargyl groups.
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