In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate.
Cell-free extracts of Burkholderia cepacia strain Pal6 catalysed the degradation of 3-phosphonopyruvate to pyruvate and inorganic phosphate; the products were detected in equimolar quantities. The stable in vitro activity responsible was distinct from both phosphonoactealdehyde hydrolase and phosphonoacetate hydrolase and from phosphoenolpyruvate phosphomutase and appears to represent a novel mode of carbon-phosphorus bond cleavage.
School of Biology and Biochemistry, The Queen's University of Belfast, Belfast, Northern Ireland. ng.ternan@ulst.ac.uk
N G
NG
Ternan
J P
JP
Quinn
D016956:Burkholderia cepacia / Q000201:enzymology*; D006090:Gram-Negative Bacteria / Q000201:enzymology; D008190:Lyases / Q000378:metabolism*; D010710:Phosphates / Q000032:analysis; D011773:Pyruvates / Q000032:analysis / Q000378:metabolism*; D013379:Substrate Specificity
C026220:3-phosphonopyruvate; D010710:Phosphates; D011773:Pyruvates; D008190:Lyases; C051328:carbon-phosphorus lyase