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Literature summary for 2.7.1.67 extracted from

  • Li, Y.S.; Porter, F.D.; Hoffman, R.M.; Deuel, T.F.
    Separation and identification of two phosphatidylinositol 4-kinase activities in bovine uterus (1989), Biochem. Biophys. Res. Commun., 160, 202-209.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Triton X-100 enzyme type I is stimulated at low concentrations, enzyme type II is stimulated by concentrations of Triton up to 1% Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
adenosine enzyme type I is resistant, enzyme type II is inhibited Bos taurus
Mn2+ above 0.5 mM Bos taurus
Triton X-100 enzyme type I is inhibited at concentrations above 0.2% Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
ATP pH 8.3, enzyme type II Bos taurus
0.25
-
ATP pH 8.3, enzyme type I Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cation required, maximal activity at 5-10 mM Bos taurus
Mn2+ optimal concentration for enzyme type I is 1-20 mM, optimal activity for enzyme type II is 0.5 mM Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
enzyme type II, gel filtration Bos taurus
200000
-
enzyme type I, gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
phosphatidylinositol 4-kinase type I and type II Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
uterus
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 1-phosphatidyl-1D-myo-inositol
-
Bos taurus ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 8 optimal stability of enzyme type I and type II Bos taurus