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In Vitro Phosphinate Methylation by PhpK from Kitasatospora phosalacinea

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posted on 2011-10-25, 00:00 authored by Williard J. Werner, Kylie D. Allen, Kaifeng Hu, Gregory L. Helms, Brian S. Chen, Susan C. Wang
Radical S-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 P-methyltransferase enzyme, PhpK, from the phosalacine producer Kitasatospora phosalacinea. PhpK catalyzes the transfer of a methyl group from methylcobalamin to 2-acetylamino-4-hydroxyphosphinylbutanoate (N-acetyldemethylphosphinothricin) to form 2-acetylamino-4-hydroxymethylphosphinylbutanoate (N-acetylphosphinothricin). This transformation gives rise to the only carbon–phosphorus–carbon linkage known to occur in Nature.

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