EC Number |
Activating Compound |
Reference |
---|
4.6.1.19 | 2',5'-linked oligoadenylates |
two different binding sites in the enzyme's ANK domain and a third site in the N lobe of the KH domain, sensing mechanism, structure-function analysis, overview. The KH/KH and kinase extension nuclease (KEN)/KEN interfaces are important in 2',5'-oligoadenylate-dependent enzyme activation |
730967 |
4.6.1.19 | 2',5'-Oligoadenylate |
- |
730509 |
4.6.1.19 | 2',5'-Oligoadenylate |
binds to and activates the enzyme. It is produced in response to viral double-stranded RNA by the 2',5'-oligoadenylate synthetase |
730313 |
4.6.1.19 | 2',5'-Oligoadenylate |
mediates the enzyme activity, absolutely required for activity |
730292 |
4.6.1.19 | 2',5'-Oligoadenylate |
the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate |
730393 |
4.6.1.19 | 2',5'-oligoadenylates |
2-5A |
683943 |
4.6.1.19 | 2'-5'-linked oligoadenylates |
natural 2'-5'-linked tetraadenylates and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogues of AMP are enzyme activators with equal potency. The enzyme is activated by the binding of 2'-5'-linked oligoadenylates to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer |
729281 |
4.6.1.19 | 2'-5'-oligoadenylate |
short polyadenylate molecules that are connected by unique 2'-5' linkages, collectively referred to as 2-5A. 2-5A induces dimerization via the ANK domain and this dimerization correlates with activation of ribonuclease activity |
729297 |
4.6.1.19 | citrate |
25 mM sodium citrate buffer results in 170% activity compared to 100% activity in sodium acetate buffer, both pH 5.6 |
656706 |
4.6.1.19 | MgCl2 |
stimulates DNA hydrolyzing activity |
683981 |