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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.11.1.3 0.005
-
3-phosphonopyruvate 25°C, pH 7.5, wild-type enzyme Variovorax sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.11.1.3 Co2+ activates, Km: 0.0061 mM Variovorax sp.
3.11.1.3 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.
3.11.1.3 Mn2+ activates, 0.00073 mM Variovorax sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.11.1.3 31000
-
4 * 31000, SDS-PAGE Variovorax sp.
3.11.1.3 110000
-
gel filtrration Variovorax sp.

Organism

EC Number Organism UniProt Comment Textmining
3.11.1.3 Variovorax sp. Q84G06
-
-
3.11.1.3 Variovorax sp. Pal2 Q84G06
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.11.1.3 recombinant Variovorax sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.11.1.3 3-phosphonopyruvate + H2O rapid equilibrium ordered kinetic mechanism with Mg2+ binding first Variovorax sp. pyruvate + phosphate
-
?
3.11.1.3 3-phosphonopyruvate + H2O rapid equilibrium ordered kinetic mechanism with Mg2+ binding first Variovorax sp. Pal2 pyruvate + phosphate
-
?
3.11.1.3 phosphoenolpyruvate + H2O
-
Variovorax sp. pyruvate + phosphate
-
?
3.11.1.3 phosphoenolpyruvate + H2O
-
Variovorax sp. Pal2 pyruvate + phosphate
-
?

Subunits

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.11.1.3 105
-
3-phosphonopyruvate 25°C, pH 7.5, wild-type enzyme Variovorax sp.
3.11.1.3 121
-
3-phosphonopyruvate 25°C, pH 7.5, mutant enzyme R188A Variovorax sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.11.1.3 0.017
-
sulfopyruvate 25°C, pH 7.5 Variovorax sp.
3.11.1.3 0.032
-
Ca2+ 25°C, pH 7.5 Variovorax sp.
3.11.1.3 0.21
-
phosphoenolpyruvate 25°C, pH 7.5 Variovorax sp.
3.11.1.3 2
-
oxalate 25°C, pH 7.5 Variovorax sp.