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Literature summary for 3.1.3.11 extracted from

  • Hines, J.K.; Fromm, H.J.; Honzatko, R.B.
    Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state (2007), J. Biol. Chem., 282, 11696-11704.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
citrate activates Escherichia coli
phosphoenolpyruvate activates Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of native and selenomethionine-substituted proteins are grown by hanging drop in vapor diffusion method, citrate-bound crystals and phosphoenolpyruvate-bound crystals Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
AMP
-
 Escherichia coli
additional information activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0014
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+ Escherichia coli
0.0017
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, assay is initiated by the addition of enzyme Escherichia coli
0.016
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A993
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
 Escherichia coli D-fructose 6-phosphate + phosphate
-
 ?

Subunits

Subunits Comment Organism
tetramer at physiologically relevant concentrations, phosphoenolpyruvate and citrate stabilize an active tetramer over a less active enzyme form of mass comparable with that of a dimer Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
8
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+ Escherichia coli
24
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, assay is initiated by the addition of enzyme Escherichia coli
26
-
 D-fructose 1,6-bisphosphate 22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+ Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0022
-
 22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+ Escherichia coli AMP
0.0181
-
 22°C, pH 7.5, assay is initiated by the addition of enzyme Escherichia coli AMP
0.02
-
 22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+ Escherichia coli AMP