bi201220r_si_001.pdf (276.81 kB)
In Vitro Phosphinate Methylation by PhpK from Kitasatospora phosalacinea
journal contribution
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. WangRadical 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.