EC Number   |
Activating Compound |
Reference |
|---|
   2.7.7.84 | dsRNA |
2'-5'-oligoadenylate synthases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. All mammalian OAS proteins require dsRNA for activity ssRNA or DNA does not activate this class of enzymes. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. OAS1 RNA activation site structure, overview |
720462 |
| 2.7.7.84 | dsRNA |
double-stranded RNA, synthetic poly(I:C), an allosteric activator of the latent (2-5)A synthetase |
723200 |
| 2.7.7.84 | dsRNA |
OAS1 can be catalytically activated by dsRNA of any length greater than 19 bp. Highly structured viral RNAs are established OAS1 activators, but they are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. In-vitro transcribtion of WNV 5' TR, WNV 3' TR, VAI, VAIDELTATS, HIV-TAR, and EBER-1 from linearized plasmids using T7 polymerase, with the exceptions of HIV-TAR and EBER-1, all viral RNAs can activate OAS1 to some extent. Whereas 5'-TR and 3'-TR achieve potent activation, VAI and VAIDELTATS are only modestly above baseline |
760514 |
| 2.7.7.84 | dsRNA |
OAS2 shows a marked increase in activity with increasing dsRNA length with a minimum requirement of 35 bp. Activation of OAS2 is also more efficient when the dsRNA contained 3'-overhangs, despite no significant impact on binding affinity. The OAS2 activation potential is dependent on dsRNA length, kinetic analysis, overview. In-vitro transcribtion of WNV 5' TR, WNV 3' TR, VAI, VAIDELTATS, HIV-TAR, and EBER-1 from linearized plasmids using T7 polymerase, none of the RNAs can activate isozyme OAS2 |
760514 |
| 2.7.7.84 | dsRNA |
the catalysis of 2'-5'-oligoadenylate synthesis is strictly dependent on double-stranded RNA and magnesium ions |
722256 |
| 2.7.7.84 | dsRNA |
the enzyme is dependent on dsRNA, activation of isozyme OAs3 by 0.001 mg/ml, and of isozymes AS1 and OAS2 by 0.1 mg/ml, at optimals pH values |
721753 |
| 2.7.7.84 | more |
highly structured viral RNAs that are established OAS1 activators are not able to activate OAS2 enzymatic activity based on the lack of extended stretches of dsRNA of greater than 35 bp. Phosphorylation state of the 5' end of dsRNA activators does not affect OAS2 activation |
760514 |
| 2.7.7.84 | viral dsRNA |
2'-5'-oligoadenylate synthases are activated by viral double-stranded RNA in infected cells and initiate a cellular response by synthesizing 2'-5'-oligoadenylates, which in turn activate RNase L. All mammalian OAS proteins require dsRNA for activity ssRNA or DNA does not activate this class of enzymes. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. OAS1 RNA activation site structure, overview |
720462 |
| 2.7.7.84 | viral RNA VAI |
sequences and secondary structures of adenovirus VAI dsRNAs, overview. Highly structured RNA, VAI, positively regulates the activity of the interferon-induced 2'5'-oligoadenylate synthase, which typically represents a key mechanism whereby host-cell protein translation is attenuated in response to foreign dsRNA. In the contrary, with other cell proteins, RNA VAI, after processing by the RNA silencing machinery, inhibits the innate immune response via a series of interactions with specific protein partners. OAS1:VAI complex stoichiometry and kinetics, overview. The RNA 5'-end phosphorylation state is important in the activation or inhibition of OAS enzymes. While full-length VAI does indeed activate OAS1 in vitro, the Dicer-truncated molecule lacking the terminal stem has the opposite effect, and this is the physiologically important response, overview |
722991 |
