Comparative -adenosyl--methionine analogue generation for selective biocatalytic Friedel-Crafts alkylation

Methyltransferases provide excellent specificity in late-stage alkylation of biomolecules. Their dependence on S -adenosyl- l -methionine (SAM) mandates efficient access to SAM analogues for biocatalytic applications. We directly compared halide methyltransferase (HMT) and methionine adenosyltransfe...

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Published inChemical communications (Cambridge, England) Vol. 59; no. 36; pp. 5463 - 5466
Main Authors Hoffmann, Arne, Schülke, Kai H, Hammer, Stephan C, Rentmeister, Andrea, Cornelissen, Nicolas V
Format Journal Article
Published 02.05.2023
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Summary:Methyltransferases provide excellent specificity in late-stage alkylation of biomolecules. Their dependence on S -adenosyl- l -methionine (SAM) mandates efficient access to SAM analogues for biocatalytic applications. We directly compared halide methyltransferase (HMT) and methionine adenosyltransferase (MAT) to access SAM analogues and explored their utility in cascade reactions with NovO for regioselective, late-stage Friedel-Crafts alkylation of a coumarin. The HMT cascade efficiently provided SAM for methylation, while the MAT cascade also supplied high levels of SAM analogues for alkylation reactions. Comparison of S -adenosyl- l -methionine (SAM) analogue generation by halide methyltransferase (HMT) and methionine adenosyltransferase (MAT) for methyltransferase catalysed alkylation.
Bibliography:https://doi.org/10.1039/d3cc01036h
Electronic supplementary information (ESI) available. See DOI
ISSN:1359-7345
1364-548X
DOI:10.1039/d3cc01036h