ISSN:
1432-072X
Keywords:
Key words Phosphonopyruvate
;
Hydrolase
;
C-P bond
;
Inducible
;
Phosphonoalanine
;
Organophosphonates
;
Deregulated
;
pho regulon
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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 °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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002030050005
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