Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Klippel, A.; Escobedo, J.A.; Hirano, M.; Williams, L.T.
    The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity (1994), Mol. Cell. Biol., 14, 2675-2685.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.153 additional information expression of regulatory protein p85 102 amino acid binding domain plus catalytic subunit p110 leads to fully active enzyme complex Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.137 85000
-
 1 * 85000 + 1 * 110000 Mus musculus
2.7.1.137 85000
-
 85000 Da subunit, previously thought to have only a linking role in localizing the p110 catalytic subunit, is an important component of the catalytic complex Mus musculus
2.7.1.137 110000
-
 1 * 85000 + 1 * 110000 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.137 Mus musculus P42337
-
-
2.7.1.153 Mus musculus P42337 recombinant enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.137 ATP + 1-phosphatidylinositol
-
 Mus musculus ADP + phosphatidylinositol 3-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.137 dimer 1 * 85000 + 1 * 110000 Mus musculus
2.7.1.137 More 85000 Da subunit, previously thought to have only a linking role in localizing the p110 catalytic subunit, is an important component of the catalytic complex Mus musculus
2.7.1.153 More interactive domains in subunits p85 and p110 responsible for binding to each other are less than 103 and 124 amino acids, respectively. Association of subunits is critical for enzyme activity Mus musculus