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, Gene, KEGG, MetaCyc, PDB |
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 17408844] |
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[EC 2.7.7.84 created 2013] |
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