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Literature summary for 3.1.3.25 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
Search for more literature for 3.1.3.25

Activating Compound

Activating Compound Comment Organism Structure
Mn2+ activating Escherichia coli

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
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
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
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
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

Organism UniProt Comment Textmining
Escherichia coli P0ADG4
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
IMPase
-
 Escherichia coli
inositol monophosphatase
-
 Escherichia coli
SuhB
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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
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
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
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
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
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
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
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
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
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
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
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