Phosphoenolpyruvate phosphomutase activity in an L-phosphonoalanine-mineralizing strain of burkholderia cepacia

A strain of Burkholderia cepacia isolated by enrichment culture utilized L-2-amino-3-phosphonopropionic acid (phosphonoalanine) at concentrations up to 20 mM as a carbon, nitrogen, and phosphorus source in a phosphate-insensitive manner. Cells contained phosphoenolpyruvate phosphomutase activity, presumed to be responsible for cleavage of the C---P bond of phosphonopyruvate, the transamination product of L-phosphonoalanine; this was inducible in the presence of phosphonoalanine.