Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.

@article{Allen2014SpectroscopicCA,
  title={Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217.},
  author={Kylie D. Allen and Susan C Wang},
  journal={Biochimica et biophysica acta},
  year={2014},
  volume={1844 12},
  pages={
          2135-44
        }
}
Natural products containing carbon-phosphorus bonds elicit important bioactivity in many organisms. l-Phosphinothricin contains the only known naturally-occurring carbon-phosphorus-carbon bond linkage. In actinomycetes, the cobalamin-dependent radical S-adenosyl-l-methionine (SAM) methyltransferase PhpK catalyzes the formation of the second C-P bond to generate the complete C-P-C linkage in phosphinothricin. Here we use electron paramagnetic resonance and nuclear magnetic resonance… Expand
Consecutive radical S-adenosylmethionine methylations form the ethyl side chain in thienamycin biosynthesis
Vitamin B12 in the spotlight again.
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