Activating Compound | Comment | Organism | Structure |
---|---|---|---|
forskolin | forskolin binds cyclase relatively weakly in the absence of the Galphas subunit. The presence of Galphas substantially increases the ability of forskolin to complement and activate the cyclase | Homo sapiens |
Application | Comment | Organism |
---|---|---|
analysis | development of a fluorescence resonance energy transfer (FRET) sensor that functions both as a soluble cyclase and a reporter of complementation within the catalytic domain. There is a strong linear correlation between catalytic domain complementation and cyclase activity upon stimulation with forskolin and the Galphas subunit. The sensor is functional in live cells | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
transfection of Sf9 cell | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2'-d3'-AMP | P-site inhibitor, uncompetitive. A complemented state of the enzyme is strongly stabilized by the presence of the inhibitor and diphosphate; P-site inhibitor, uncompetitive. A complemented state of the enzyme is strongly stabilized by the presence of the inhibitor and diphosphate | Homo sapiens | |
additional information | presence of diphosphate does not have a significant effect on either cyclase activity or FRET; presence of diphosphate does not have a significant effect on either cyclase activity or FRET | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O95622 | isoform Adcy5 | - |
Homo sapiens | Q08462 | isoform Adcy2 | - |