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Literature summary for 2.7.1.67 extracted from

  • Saha, A.K.; Dowling, J.N.; Mukhopadhyay, N.K.; Glew, R.H.
    Legionella micdadei protein kinase catalyzes phosphorylation of tubulin and phosphatidylinositol (1989), J. Bacteriol., 171, 5103-5110.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
octyl beta-D-glucoside 10-20 mM, stimulates Tatlockia micdadei
Triton X-100 0.25-0.5%, stimulates Tatlockia micdadei

Inhibitors

Inhibitors Comment Organism Structure
phosphatidylcholine 0.6 mM, 45% inhibition Tatlockia micdadei
phosphatidylethanolamine 0.6 mM, 67% inhibition Tatlockia micdadei
phosphatidylglycerol 0.6 mM, 68% inhibition Tatlockia micdadei
phosphatidylinositol 4,5-bisphosphate 0.6 mM, 50% inhibition Tatlockia micdadei
phosphatidylinositol 4-phosphate 0.6 mM, 80% inhibition Tatlockia micdadei
phosphatidylserine 0.6 mM, 28% inhibition Tatlockia micdadei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5
-
ATP pH 7.2, 37°C Tatlockia micdadei

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ divalent cation requirement is best satisfied by Mg2+ and Ca2+ Tatlockia micdadei
Mg2+ divalent cation requirement is best satisfied by Mg2+ and Ca2+ Tatlockia micdadei

Organism

Organism UniProt Comment Textmining
Tatlockia micdadei
-
-
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Tatlockia micdadei