Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6.

Abstract

A novel, inducible carbon-phosphorus bond cleavage enzyme, phosphonopyruvate hydrolase, was detected in cell-free extracts of Burkholderia cepacia Pal6, an environmental isolate capable of mineralising L-phosphonoalanine as carbon, nitrogen and phosphorus source. The activity was induced only in the presence of phosphonoalanine, did not require phosphate starvation for induction and was uniquely specific for phosphonopyruvate, producing equimolar quantities of pyruvate and inorganic phosphate. The native enzyme had a molecular mass of some 232 kDa and showed activation by metal ions in the order Co2+ > Ni2+ > Mg2+ > Zn2+ > Fe2+ > Cu2+. Temperature and pH optima in crude cell extracts were 50 degrees C and 7.5, respectively, and activity was inhibited by EDTA, phosphite, sulfite, mercaptoethanol and sodium azide. Phosphonopyruvate hydrolase is the third bacterial C-P bond cleavage enzyme reported to date that proceeds via a hydrolytic mechanism.

• Authors: N G Ternan, J T Hamilton, J P Quinn
• Journal: Archives of microbiology (Arch Microbiol) Vol. 173 Issue 1 Pg. 35-41 (Jan 2000) ISSN: 0302-8933 [Print] Germany
• PMID: 10648102 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Organophosphorus Compounds
• Hydrolases
• Phosphotransferases (Phosphomutases)
• phosphoenolpyruvate mutase

Topics

• Burkholderia cepacia (enzymology)
• Enzyme Stability
• Hydrogen-Ion Concentration
• Hydrolases (metabolism)
• Organophosphorus Compounds (metabolism)
• Phosphotransferases (Phosphomutases) (metabolism)
• Substrate Specificity
• Temperature