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Literature summary extracted from

  • Brown, G.; Singer, A.; Lunin, V.V.; Proudfoot, M.; Skarina, T.; Flick, R.; Kochinyan, S.; Sanishvili, R.; Joachimiak, A.; Edwards, A.M.; Savchenko, A.; Yakunin, A.F.
    Structural and biochemical characterization of the type II D-fructose-1,6-bisphosphatase GlpX from Escherichia coli (2009), J. Biol. Chem., 284, 3784-3792.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.11 DTT increases activity by 40-50% Escherichia coli
3.1.3.11 KCl slightly increases activity by 20% Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 expressed in Escherichia coli as a His-tagged fusion protein Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.11 crystal structure of GlpX is determined in a free state and in the complex with a D-fructose 1,6-bisphosphate or inhibitor (phosphate). The crystal structure of the ligand-free GlpX reveals a compact, globular shape with two alpha/beta-sandwich domains. The core fold of GlpX is structurally similar to that of Li+-sensitive phosphatases implying that they have a common evolutionary origin and catalytic mechanism. The structure of the GlpX complex with D-fructose 1,6-bisphosphate reveals that the active site is located between two domains and accommodates several conserved residues coordinating two metal ions and the substrate. The third metal ion is bound to phosphate 6 of the substrate. Phosphate (inhibitor) binds to the active site Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 D186A Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.2 (wild-type: 5.7/sec) Escherichia coli
3.1.3.11 E59A Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.1 (wild-type: 5.7/sec) Escherichia coli
3.1.3.11 K239A Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 7.5 (wild-type: 5.7/sec) Escherichia coli
3.1.3.11 K29A Km (mM) (D-fructose 1,6-bisphosphate): 0.06 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 14 (wild-type: 5.7/sec) Escherichia coli
3.1.3.11 R235A Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 5.4 (wild-type: 5.7/sec) Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 ATP 1 mM, reduces activity by 40% Escherichia coli
3.1.3.11 KCl 50 mM, residual activity 20% Escherichia coli
3.1.3.11 LiCl
-
 Escherichia coli
3.1.3.11 phosphate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.06
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant K29A Escherichia coli
3.1.3.11 0.07
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, wild-type Escherichia coli
3.1.3.11 0.1
-
 fructose 1,6-bisphosphate wild-type Escherichia coli
3.1.3.11 0.1
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant E59A Escherichia coli
3.1.3.11 0.1
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant K239A Escherichia coli
3.1.3.11 0.2
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant D186A Escherichia coli
3.1.3.11 0.2
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant R235A Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.11 KCl 50 mM, 20% stimulation Escherichia coli
3.1.3.11 Mn2+ divalent metal cations are required for enzymatic activity. However, only Mn2+ supports activity of GlpX and YggF Escherichia coli
3.1.3.11 Mn2+ divalent metal cations are required for enzymatic activity. Mn2+ supports activity of GlpX and YggF Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.11 34300
-
 2 * 34300, calculated from sequence Escherichia coli
3.1.3.11 36000
-
 2 * 36000, calculated from sequence Escherichia coli
3.1.3.11 76000
-
 dimer, gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Escherichia coli P0A9C9 Escherichia coli has two class II D-fructose 1,6-bisphosphatase GlpX and YggF
-
3.1.3.11 Escherichia coli P21437 uncharacterized protein YggF; Escherichia coli has two class II fructose 1,6-bisphosphatase GlpX and YggF
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11 using Ni-NTA chromatography Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.1.3.11 homodimer 2 * 34300, calculated from sequence Escherichia coli
3.1.3.11 homodimer 2 * 36000, calculated from sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.3.11 D-fructose 1,6-bisphosphatase
-
 Escherichia coli
3.1.3.11 fructose 1,6-bisphosphatase
-
 Escherichia coli
3.1.3.11 GlpX
-
 Escherichia coli
3.1.3.11 YggF
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.11 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 1.1
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant E59A Escherichia coli
3.1.3.11 1.2
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant D186A Escherichia coli
3.1.3.11 2.5
-
 fructose 1,6-bisphosphate wild-type Escherichia coli
3.1.3.11 5.4
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant R235A Escherichia coli
3.1.3.11 5.7
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, wild-type Escherichia coli
3.1.3.11 7.5
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant K239A Escherichia coli
3.1.3.11 14
-
 D-fructose 1,6-bisphosphate pH 9.0, 37°C, mutant K29A Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.11 7.5
-
 pH optimum: 7.5-8.0 Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.1.3.11 1.2
-
-
 Escherichia coli phosphate
3.1.3.11 3
-
-
 Escherichia coli phosphate
3.1.3.11 15.8
-
-
 Escherichia coli LiCl
3.1.3.11 70
-
-
 Escherichia coli LiCl