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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
phosphonopyruvate hydrolase,
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PalA
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PPH
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3-phosphonopyruvate + H2O = pyruvate + phosphate
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3-phosphonopyruvate + H2O
pyruvate + phosphate
phosphoenolpyruvate + H2O
enolpyruvate + phosphate
3-phosphonopyruvate + H2O
pyruvate + phosphate
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-
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
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the activity is induced in presence of phosphonoalanine and does not require phosphate starvation for induction
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?
3-phosphonopyruvate + H2O
pyruvate + phosphate
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-
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
-
the activity is induced in presence of phosphonoalanine and does not require phosphate starvation for induction
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
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-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
the enzyme is likely to be of considerable significance in global phosphorous cycling, because phosphonopyruvate is known to be a key intermediate in the formation of all naturally occuring compounds that cotain the carbon-phosphorus bond
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
rapid equilibrium ordered kinetic mechanism with Mg2+ binding first
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?
3-phosphonopyruvate + H2O
pyruvate + phosphate
rapid equilibrium ordered kinetic mechanism with Mg2+ binding first
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?
3-phosphonopyruvate + H2O
pyruvate + phosphate
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-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
the enzyme is likely to be of considerable significance in global phosphorous cycling, because phosphonopyruvate is known to be a key intermediate in the formation of all naturally occuring compounds that cotain the carbon-phosphorus bond
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?
phosphoenolpyruvate + H2O
enolpyruvate + phosphate
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-
?
phosphoenolpyruvate + H2O
enolpyruvate + phosphate
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-
?
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3-phosphonopyruvate + H2O
pyruvate + phosphate
3-phosphonopyruvate + H2O
pyruvate + phosphate
-
the activity is induced in presence of phosphonoalanine and does not require phosphate starvation for induction
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-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
-
the activity is induced in presence of phosphonoalanine and does not require phosphate starvation for induction
-
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
the enzyme is likely to be of considerable significance in global phosphorous cycling, because phosphonopyruvate is known to be a key intermediate in the formation of all naturally occuring compounds that cotain the carbon-phosphorus bond
-
-
?
3-phosphonopyruvate + H2O
pyruvate + phosphate
the enzyme is likely to be of considerable significance in global phosphorous cycling, because phosphonopyruvate is known to be a key intermediate in the formation of all naturally occuring compounds that cotain the carbon-phosphorus bond
-
-
?
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Ca2+
-
5 mM, 1.5fold activation
Cu2+
-
5 mM, 1.2fold activation
Mn2+
activates, 0.00073 mM
Zn2+
-
5 mM, 1.8fold activation
Co2+
-
5 mM, 4.8fold activation
Co2+
5 mM, 2.27fold activation
Co2+
activates, Km: 0.0061 mM
Mg2+
-
5 mM, 3.4fold activation
Mg2+
5 mM, 1.43fold activation
Mg2+
activates, Km: 0.0035 mM. The Mg2+-binding is formed by the carboxylate groups of ASp54, Asp81, Asp83 and Glu110, with ASp81 coordinating directly to the metal, and the remaining carboxylate groups bridged by water molecules
Ni2+
-
5 mM, 4.3fold activation
Ni2+
5 mM, 1.54fold activation
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3-phosphonopropionic acid
Aminomethylphosphonic acid
-
10 mM, 19% inhibition
Cu2+
5 mM, 41% loss of activity
Fe2+
-
5 mM, 94% inhibition
glyphosate
-
10 mM, 23% inhibition
hydroxymethylphosphonic acid
5 mM, 25% loss of activity
phosphoenolpyruvate
competitive
Phosphonoacetate
-
10 mM, 30% inhibition
phosphonobutyric acid
-
10 mM, 14% inhibition
Phosphonoformate
-
10 mM, 37% inhibition
Phosphonoformic acid
5 mM, 76% loss of activity
sulfopyruvate
competitive
3-phosphonopropionic acid
-
10 mM, 21% inhibition
3-phosphonopropionic acid
5 mM, 17% loss of activity
EDTA
-
Co2+, Ni2+, Mg2+, Zn2+, Fe3+ and Ca2+ recover activity. Cu2+, Mn2+ and Cs+ do not recover activity
Mn2+
-
5 mM, 12% inhibition
Mn2+
5 mM, 41% loss of activity
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additional information
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phosphonopyruvate and phosphonoalanine induce the enzyme in strain Pal2
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0.005 - 0.72
3-phosphonopyruvate
0.005
3-phosphonopyruvate
25°C, pH 7.5, wild-type enzyme
0.53
3-phosphonopyruvate
37°C
0.72
3-phosphonopyruvate
-
-
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105 - 121
3-phosphonopyruvate
105
3-phosphonopyruvate
25°C, pH 7.5, wild-type enzyme
121
3-phosphonopyruvate
25°C, pH 7.5, mutant enzyme R188A
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0.21
phosphoenolpyruvate
25°C, pH 7.5
0.017
sulfopyruvate
25°C, pH 7.5
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5.35
isoelectric focusing
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brenda
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brenda
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SwissProt
brenda
gene palA
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-
brenda
Pal2
SwissProt
brenda
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SwissProt
brenda
gene palA
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-
brenda
Pal2
SwissProt
brenda
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the enzyme is expressed even in the presence of high levels of phosphate, thus permitting phosphonopyruvate to be used as the sole carbon and energy source
brenda
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the enzyme is expressed even in the presence of high levels of phosphate, thus permitting phosphonopyruvate to be used as the sole carbon and energy source
brenda
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Variovorax sp. (strain Pal2)
Variovorax sp. (strain Pal2)
Variovorax sp. (strain Pal2)
Variovorax sp. (strain Pal2)
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232000
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non-denaturing PAGE
31000
4 * 31000, SDS-PAGE
31187
2 * 31187, mass spectrometry
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dimer
2 * 31187, mass spectrometry
dimer
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2 * 31187, mass spectrometry
tetramer
4 * 31000, SDS-PAGE
tetramer
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4 * 31000, SDS-PAGE
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hanging drop vapour diffusion method, enzyme in unbound state and in complex with Mg2+ and the inhibitor oxalate
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R188A
1.15fold increase in turnover number
R188A
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1.15fold increase in turnover number
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50
10 min, loss of activity
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dialysis of cell-free extract for 24 h at 4°C results in a 72% loss of activity
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-20°C, 10 weeks, 54% loss of activity
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-20°C, 25% glycerol, 6 months, about 20% loss of activity
20, 50% loss of activity after 3 days, complete loss of activity after 6 days
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4°C, 30 days, 38% loss of activity
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expression in Escherichia coli
gene palA, DNA and amino acid sequence determination and analysis, the palA gene is organized with four other structural genes, genes palA, palB, palC, palD and palE, in the 2-amino-3-phosphonopropionic acid (phosphonoalanine)-degradative operon, overview. Expression of GFP-tagged PalA, with or without coexpression of the other genes of the operon, in Pseudomonas putida strain KT2440
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Ternan, N.G.; Hamilton, J.T.; Quinn, J.P.
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
Burkholderia cepacia, Burkholderia cepacia Pal6
brenda
Chen, C.C.; Han, Y.; Niu, W.; Kulakova, A.N.; Howard, A.; Quinn, J.P.; 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
11491-11504
2006
Variovorax sp. (Q84G06), Variovorax sp. Pal2 (Q84G06)
brenda
Kulakova, A.N.; Wisdom, G.B.; Kulakov, L.A.; Quinn, J.P.
The purification and characterization of phosphonopyruvate hydrolase, a novel carbon-phosphorus bond cleavage enzyme from Variovorax sp Pal2
J. Biol. Chem.
278
23426-23431
2003
Variovorax sp. (Q84G06), Variovorax sp. Pal2 (Q84G06)
brenda
Kulakova, A.N.; Kulakov, L.A.; Villarreal-Chiu, J.F.; Gilbert, J.A.; McGrath, J.W.; Quinn, J.P.
Expression of the phosphonoalanine-degradative gene cluster from Variovorax sp. Pal2 is induced by growth on phosphonoalanine and phosphonopyruvate
FEMS Microbiol. Lett.
292
100-106
2009
Variovorax sp., Variovorax sp. Pal2
brenda
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3.11.1.3 phosphonopyruvate hydrolase
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