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.
Ternan
NG
School of Biology and Biochemistry, The Queen's University of Belfast, Belfast, Northern Ireland.
McGrath
JW
Quinn
JP