EC Number   |
Activating Compound |
Reference |
|---|
   2.7.7.65 | 4-(5-[(E)-[2-(4-amino-1,2,5-oxadiazole-3-carbonyl)hydrazinylidene]methyl]furan-2-yl)benzoic acid |
18% activation at 0.1 mM |
761378 |
| 2.7.7.65 | 4-chloro-N'-[(E)-(4-cyanophenyl)methylidene]-3-nitrobenzene-1-sulfonohydrazide |
15% activation at 0.1 mM |
761378 |
| 2.7.7.65 | 4-[(E)-[2-(4-hydroxy-6-methylpyrimidin-2-yl)hydrazinylidene]methyl]phenyl 3-nitrobenzoate |
8% activation at 0.1 mM |
761378 |
| 2.7.7.65 | 4-[(E)-[2-(4-sulfamoylphenyl)hydrazinylidene]methyl]benzoic acid |
6% activation at 0.1 mM |
761378 |
| 2.7.7.65 | acetyl phosphate |
- |
725263 |
| 2.7.7.65 | BeF3- |
- |
705162 |
| 2.7.7.65 | beryllium fluoride |
BeF3, phosphoryl mimic, optimum concentration: 1 mM BeCl2/10 mM NaF (nonspecifcally inhibitory at higher concentrations), causes dimerisation and cyclic di-3,5-guanylate synthesis, no influence on cyclic-di-GMP binding affinity and thus allosteric regulation |
680826 |
| 2.7.7.65 | beryllium fluoride |
BeF3-, pseudo-phosphorylation, enhances dimerisation by lowering KD to less than 10 microM, tightens dimer interface between two D1/D2 domains, modification activates enzyme |
682885 |
| 2.7.7.65 | cAMP |
required, Lcd1 DGC activity is negligible in the absence of cAMP and is significantly enhanced in its presence. The GAF domain binds specifically cAMP and has an important role in the regulation of the DGC activity of the GGDEF domain. cAMP binding site and specificity, overview |
761695 |
| 2.7.7.65 | more |
membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers |
760992 |
