The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity .
Kerr, I.M. and Brown, R.E. pppA2′p5’A2′p5’A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells. Proc. Natl. Acad. Sci. USA75 (1978) 256–260. [DOI] [PMID: 272640]
Martin, E.M., Birdsall, N.J., Brown, R.E. and Kerr, I.M. Enzymic synthesis, characterisation and nuclear-magnetic-resonance spectra of pppA2′p5’A2′p5’A and related oligonucleotides: comparison with chemically synthesised material. Eur. J. Biochem.95 (1979) 295–307. [DOI] [PMID: 456356]
Hartmann, R., Justesen, J., Sarkar, S.N., Sen, G.C. and Yee, V.C. Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′-oligoadenylate synthetase. Mol. Cell12 (2003) 1173–1185. [DOI] [PMID: 14636576]
Hovanessian, A.G. and Justesen, J. The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie89 (2007) 779–788. [DOI] [PMID: 17408844]