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Literature summary for 3.1.4.4 extracted from

  • Edwards, J.L.; Apicella, M.A.
    Neisseria gonorrhoeae PLD directly interacts with Akt kinase upon infection of primary, human, cervical epithelial cells (2006), Cell. Microbiol., 8, 1253-1271.
    View publication on PubMed
Search for more literature for 3.1.4.4

Application

Application Comment Organism
medicine enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling Neisseria gonorrhoeae

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Neisseria gonorrhoeae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Neisseria gonorrhoeae enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling ?
-
 ?

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme augments gonococcus invasion of cervical epithelia by interacting with Akt kinase in a hosphatidylinositol-(3,4,5)-trisphosphate-independent manner, resulting in subversion of normal cervical cell signaling Neisseria gonorrhoeae ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme directly binds to the PH domain of Akt kinase and can compete with natural Akt ligand phosphatidylinositol-(3,4,5)-trisphosphate for Akt binding Neisseria gonorrhoeae