In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea - PubMed (original) (raw)

. 2011 Oct 25;50(42):8986-8.

doi: 10.1021/bi201220r. Epub 2011 Sep 28.

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In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea

Williard J Werner et al. Biochemistry. 2011.

Abstract

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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Figures

Figure 1

Figure 1

H-P gHSQC spectrum of the partially purified 13CH3-Cbl(III) PhpK reaction. The 13CH3 H-P crosspeaks are centered at (1.15, 43.1) ppm (designated by the “x”).

Scheme 1

Scheme 1

Proposed P-methyl transfer reactions

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