An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases.

@article{Hendricks2004AnEC,
  title={An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases.},
  author={Cheryl L Hendricks and Jeannine R Ross and Eran Pichersky and Joseph P Noel and Zhaohui Sunny Zhou},
  journal={Analytical biochemistry},
  year={2004},
  volume={326 1},
  pages={100-5}
}
We report here an enzyme-coupled colorimetric assay for salicylic acid carboxyl methyltransferase (SAMT), which utilizes S-adenosyl-l-methionine (AdoMet or SAM) as the methyl donor. In this assay, S-adenosyl-l-homocysteine (AdoHcy or SAH), a common product of AdoMet-dependent transmethylation reactions, is first hydrolyzed by recombinant AdoHcy nucleosidase (EC 3.2.2.9) into adenine and S-ribosylhomocysteine. Recombinant LuxS (S-ribosylhomocysteinase, EC 3.2.1.148) cleaves the latter compound… CONTINUE READING