期刊
BIOCHEMISTRY
卷 50, 期 42, 页码 8986-8988出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi201220r
关键词
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资金
- National Institutes of Health (NIH) [P41RR02301, RR02781, RR08438, RR0631401, RR12948, T32GM008336]
- NIGMS [P41GM66326]
- University of Wisconsin
- National Science Foundation (NSF) [DMB-8415048, OIA-9977486, BIR-9214394, CHE-9115282, DBI-9604689, CHE-0953721]
- U.S. Department of Agriculture
- Murdock Charitable Trust
- Washington State University
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0953721] Funding Source: National Science Foundation
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-acetylde-methylphosphinothricin) 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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