A tandem chemoenzymatic methylation by S-adenosyl-L-methionine

Chembiochem. 2013 May 27;14(8):950-3. doi: 10.1002/cbic.201300221. Epub 2013 May 6.

Abstract

Keep 'em methylated: The in situ preparation of the cofactor AdoMet was achieved by allowing the biosynthetic enzyme SalL to operate in the reverse direction by presentation of 5'-chloro-5'-deoxyadenosine at low salt concentrations. This reaction was readily coupled with DNA and small molecule methyltransferases to afford a regioselective method for chemo-enzymatic methylation and isotope incorporation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology
  • Methylation
  • Methyltransferases / metabolism
  • Micromonosporaceae / enzymology
  • Models, Molecular
  • S-Adenosylmethionine / chemistry
  • S-Adenosylmethionine / metabolism*

Substances

  • S-Adenosylmethionine
  • Methyltransferases