title: A tandem chemoenzymatic methylation by S-adenosyl-L-methionine.
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.
authors: Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0358, USA.
authors: Joseph M
authors: JM
authors: Lipson
authors: Marie
authors: M
authors: Thomsen
authors: Bradley S
authors: BS
authors: Moore
authors: Rasmus P
authors: RP
authors: Clausen
authors: James J
authors: JJ
authors: La Clair
authors: Michael D
authors: MD
authors: Burkart
mesh_terms: D000192:Actinomycetales / Q000201:enzymology; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D008848:Micromonosporaceae / Q000201:enzymology; D008958:Models, Molecular; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D012436:S-Adenosylmethionine; D008780:Methyltransferases
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