Werner, Williard J. Allen, Kylie D. Hu, Kaifeng Helms, Gregory L. Chen, Brian S. Wang, Susan C. In Vitro Phosphinate Methylation by PhpK from <i>Kitasatospora phosalacinea</i> Radical <i>S</i>-adenosyl-l-methionine, cobalamin-dependent methyltransferases have been proposed to catalyze the methylations of unreactive carbon or phosphorus atoms in antibiotic biosynthetic pathways. To date, none of these enzymes has been purified or shown to be active in vitro. Here we demonstrate the activity of the <i>P</i>-methyltransferase enzyme, PhpK, from the phosalacine producer <i>Kitasatospora phosalacinea</i>. PhpK catalyzes the transfer of a methyl group from methylcobalamin to 2-acetylamino-4-hydroxyphosphinylbutanoate (<i>N</i>-acetyldemethylphosphinothricin) to form 2-acetylamino-4-hydroxymethylphosphinylbutanoate (<i>N</i>-acetylphosphinothricin). This transformation gives rise to the only carbon–phosphorus–carbon linkage known to occur in Nature. methyl group;antibiotic biosynthetic pathways;PhpK catalyzes;unreactive carbon;acetylamino;phosalacine producer Kitasatospora phosalacinea;enzyme;Vitro Phosphinate Methylation;phosphorus atoms 2011-10-25
    https://acs.figshare.com/articles/journal_contribution/In_Vitro_Phosphinate_Methylation_by_PhpK_from_i_Kitasatospora_phosalacinea_i_/2594482
10.1021/bi201220r.s001