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In vitro phosphinate methylation by PhpK from Kitasatospora phosalacinea.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Werner WJ,Allen KD,Hu K,Helms GL,Chen BS,Wang SC

doi

10.1021/bi201220r

subject

Has Abstract

pub_date

2011-10-25 00:00:00

pages

8986-8

issue

42

eissn

0006-2960

issn

1520-4995

journal_volume

50

pub_type

杂志文章

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