Literature summary for 3.11.1.3 extracted from

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 (2006), Biochemistry, 45, 11491-11504.

Search for more literature for 3.11.1.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Variovorax sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapour diffusion method, enzyme in unbound state and in complex with Mg2+ and the inhibitor oxalate	Variovorax sp.

Protein Variants

Protein Variants	Comment	Organism
R188A	1.15fold increase in turnover number	Variovorax sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	competitive	Variovorax sp.
oxalate	competitive	Variovorax sp.
phosphoenolpyruvate	competitive	Variovorax sp.
sulfopyruvate	competitive	Variovorax sp.

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.005	-	3-phosphonopyruvate	25°C, pH 7.5, wild-type enzyme	Variovorax sp.

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	activates, Km: 0.0061 mM	Variovorax sp.
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	Variovorax sp.
Mn2+	activates, 0.00073 mM	Variovorax sp.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
31000	-	4 * 31000, SDS-PAGE	Variovorax sp.
110000	-	gel filtrration	Variovorax sp.

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
recombinant	Variovorax sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-phosphonopyruvate + H2O	rapid equilibrium ordered kinetic mechanism with Mg2+ binding first	Variovorax sp.	pyruvate + phosphate	-	?
3-phosphonopyruvate + H2O	rapid equilibrium ordered kinetic mechanism with Mg2+ binding first	Variovorax sp. Pal2	pyruvate + phosphate	-	?
phosphoenolpyruvate + H2O	-	Variovorax sp.	pyruvate + phosphate	-	?
phosphoenolpyruvate + H2O	-	Variovorax sp. Pal2	pyruvate + phosphate	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 31000, SDS-PAGE	Variovorax sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
105	-	3-phosphonopyruvate	25°C, pH 7.5, wild-type enzyme	Variovorax sp.
121	-	3-phosphonopyruvate	25°C, pH 7.5, mutant enzyme R188A	Variovorax sp.

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.017	-	sulfopyruvate	25°C, pH 7.5	Variovorax sp.
0.032	-	Ca2+	25°C, pH 7.5	Variovorax sp.
0.21	-	phosphoenolpyruvate	25°C, pH 7.5	Variovorax sp.
2	-	oxalate	25°C, pH 7.5	Variovorax sp.

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Release 2023.1 (January 2023)