In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate

Nigel Ternan, JP Quinn

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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. (C) 1998 Academic Press.
LanguageEnglish
Pages378-381
JournalBiochemical and biophysical research communications
Volume248
Issue number2
DOIs
Publication statusPublished - Jul 1998

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Burkholderia cepacia
Hydrolases
Cell Extracts
Pyruvic Acid
Phosphorus
Carbon
Phosphates
In Vitro Techniques
phosphoenolpyruvate mutase
phosphonoacetate hydrolase
3-phosphonopyruvate

Cite this

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abstract = "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. (C) 1998 Academic Press.",
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In vitro cleavage of the carbon-phosphorus bond of phosphonopyruvate by cell extracts of an environmental Burkholderia cepacia isolate. / Ternan, Nigel; Quinn, JP.

Vol. 248, No. 2, 07.1998, p. 378-381.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Ternan, Nigel

AU - Quinn, JP

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AB - 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. (C) 1998 Academic Press.

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