The Enzyme Database

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EC 2.7.7.84     
Accepted name: 2′-5′ oligoadenylate synthase
Reaction: 3 ATP = pppA2′p5’A2′p5’A + 2 diphosphate
Glossary: pppA2′p5’A2′p5’A = 5′-triphosphoadenylyl-(2′→5′)-adenylyl-(2′→5′)-adenosine
Other name(s): OAS
Systematic name: ATP:ATP adenylyltransferase (2′-5′ linkages-forming)
Comments: 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 [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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. USA 75 (1978) 256–260. [PMID: 272640]
2.  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. [PMID: 456356]
3.  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. Cell 12 (2003) 1173–1185. [PMID: 14636576]
4.  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. Biochimie 89 (2007) 779–788. [PMID: 17408844]
[EC 2.7.7.84 created 2013]
 
 


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