Chemoenzymatic synthesis and utilization of a SAM analog with an isomorphic nucleobase.
SalL, an enzyme that catalyzes the synthesis of SAM from l-methionine and 5'-chloro-5'-deoxyoadenosine, is shown to accept 5'-chloro-5'-deoxythienoadenosine as a substrate and facilitate the synthesis of a synthetic SAM analog with an unnatural nucleobase. This synthetic cofactor is demonstrated to replace SAM in the DNA methylation reaction with M.TaqI.
Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Heverlee, Belgium.
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Vranken
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Fin
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Tufar
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Hofkens
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Burkart
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Tor
D000241:Adenosine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D055162:Biocatalysis; D008715:Methionine / Q000737:chemistry / Q000378:metabolism; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D012436:S-Adenosylmethionine / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism*
D012436:S-Adenosylmethionine; D008715:Methionine; D008780:Methyltransferases; D000241:Adenosine