Literature summary for 3.11.1.3 extracted from

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 (2003), J. Biol. Chem., 278, 23426-23431.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Variovorax sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
3-phosphonopropionic acid	5 mM, 17% loss of activity	Variovorax sp.
Cu2+	5 mM, 41% loss of activity	Variovorax sp.
EDTA	-	Variovorax sp.
hydroxymethylphosphonic acid	5 mM, 25% loss of activity	Variovorax sp.
Mn2+	5 mM, 41% loss of activity	Variovorax sp.
Phosphonoformic acid	5 mM, 76% loss of activity	Variovorax sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.53	-	3-phosphonopyruvate	37°C	Variovorax sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	5 mM, 2.27fold activation	Variovorax sp.
Mg2+	5 mM, 1.43fold activation	Variovorax sp.
Ni2+	5 mM, 1.54fold activation	Variovorax sp.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
31187	-	2 * 31187, mass spectrometry	Variovorax sp.
63000	-	gel filtration	Variovorax sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3-phosphonopyruvate + H2O	Variovorax sp.	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	pyruvate + phosphate	-	?
3-phosphonopyruvate + H2O	Variovorax sp. Pal2	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	pyruvate + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Variovorax sp.	Q84G06	Pal2	-
Variovorax sp. Pal2	Q84G06	Pal2	-

Purification (Commentary)

Purification (Comment)	Organism
-	Variovorax sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
163	-	-	Variovorax sp.

Storage Stability

Storage Stability	Organism
-20°C, 25% glycerol, 6 months, about 20% loss of activity	Variovorax sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-phosphonopyruvate + H2O	-	Variovorax sp.	pyruvate + phosphate	-	?
3-phosphonopyruvate + H2O	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	Variovorax sp.	pyruvate + phosphate	-	?
3-phosphonopyruvate + H2O	-	Variovorax sp. Pal2	pyruvate + phosphate	-	?
3-phosphonopyruvate + H2O	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	Variovorax sp. Pal2	pyruvate + phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 31187, mass spectrometry	Variovorax sp.

Synonyms

Synonyms	Comment	Organism
PPH	-	Variovorax sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
50	-	10 min, loss of activity	Variovorax sp.

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.7	7	-	Variovorax sp.

pI Value

Organism	Comment	pI Value Maximum	pI Value
Variovorax sp.	isoelectric focusing	-	5.35

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Release 2023.1 (January 2023)