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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Neisseria gonorrhoeae | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Neisseria gonorrhoeae | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|
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 | 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 |