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Literature summary extracted from

  • Wang, Y.; Stieglitz, K.A.; Bubunenko, M.; Court, D.L.; Stec, B.; Roberts, M.F.
    The structure of the R184A mutant of the inositol monophosphatase encoded by suhB and implications for its functional interactions in Escherichia coli (2007), J. Biol. Chem., 282, 26989-26996.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.25 Mn2+ activating Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.25 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.25 the mutant protein R184A, which has equivalent IMPase activity to native SuhB, crystallizes under three different conditions: (1) 0.2 M ammonium iodide, 20% PEG 3350, pH6.2, (2) 0.2 M potassium acetate, 20% PEG 3350, pH 7.8, and (3) 0.2 M ammonium acetate, 20% PEG 3350, pH 7.1 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.25 G173V loss of sensitivity to RNA pol binding Escherichia coli
3.1.3.25 H98F slightly increased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 K251A decreased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 L96F/R184I loss of sensitivity to RNA pol binding Escherichia coli
3.1.3.25 R121A slightly decreased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 R183a increased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 R184A shift of the monomer-dimer equilibrium toward monomer Escherichia coli
3.1.3.25 R184I loss of sensitivity to RNA pol binding Escherichia coli
3.1.3.25 R199A decreased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 R248A strongly increased kcat value compared to the wild type enzyme Escherichia coli
3.1.3.25 V249A decreased kcat value compared to the wild type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.25 0.06
-
 D-myo-Inositol 1-phosphate mutant enzyme V249A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.11
-
 D-myo-Inositol 1-phosphate wild type enzyme, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.13
-
 D-myo-Inositol 1-phosphate mutant enzyme R121A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.13
-
 D-myo-Inositol 1-phosphate mutant enzyme R248A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.16
-
 D-myo-Inositol 1-phosphate mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.17
-
 D-myo-Inositol 1-phosphate mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.29
-
 D-myo-Inositol 1-phosphate mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.25 Escherichia coli P0ADG4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.25 Sephadex Q-Sepharose fast flow column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.25 D-myo-inositol 1-phosphate + H2O preferred substrate Escherichia coli D-myo-inositol + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.25 dimer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.1.3.25 IMPase
-
 Escherichia coli
3.1.3.25 inositol monophosphatase
-
 Escherichia coli
3.1.3.25 SuhB
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.25 0.165
-
 D-myo-Inositol 1-phosphate mutant enzyme K251A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.175
-
 D-myo-Inositol 1-phosphate mutant enzyme V249A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.199
-
 D-myo-Inositol 1-phosphate mutant enzyme R199A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.267
-
 D-myo-Inositol 1-phosphate mutant enzyme R248A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.357
-
 D-myo-Inositol 1-phosphate mutant enzyme R184I, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.369
-
 D-myo-Inositol 1-phosphate mutant enzyme R121A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.49
-
 D-myo-Inositol 1-phosphate wild type enzyme, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.504
-
 D-myo-Inositol 1-phosphate mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 0.747
-
 D-myo-Inositol 1-phosphate mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 1.183
-
 D-myo-Inositol 1-phosphate mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 6.08
-
 D-myo-Inositol 1-phosphate mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 6.08
-
 D-myo-Inositol 1-phosphate mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli
3.1.3.25 6.08
-
 D-myo-Inositol 1-phosphate mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C Escherichia coli