EC 188.8.131.52 Enzyme
Acting on carbon-phosphorus bonds;
Acting on carbon-phosphorus bonds (only sub-subclass identified to date)
3-phosphonopyruvate + H2O = pyruvate + phosphate [RN:
Highly specific for phosphonopyruvate as substrate . The reaction is not inhibited by phosphate but is inhibited by the phosphonates phosphonoformic acid, hydroxymethylphosphonic acid and 3-phosphonopropanoic acid . The enzyme is activated by the divalent cations Co2+, Mg2+ and Mn2+. This enzyme is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily .
EC 184.108.40.206 created 2007
Phosphonate and phosphinate metabolism
Ternan NG, Hamilton JT, Quinn JP.
Initial in vitro characterisation of phosphonopyruvate hydrolase, a novel phosphate starvation-independent, carbon-phosphorus bond cleavage enzyme in Burkholderia cepacia Pal6.
Arch Microbiol 173:35-41 (2000)
Kulakova AN, Wisdom GB, Kulakov LA, Quinn JP
The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2.
J Biol Chem 278:23426-31 (2003)
Chen CC, Han Y, Niu W, Kulakova AN, Howard A, Quinn JP, Dunaway-Mariano D, Herzberg O
Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily.
Biochemistry 45:11491-504 (2006)
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