Reactome | Gel filtration experiments using extracts from IFN-treated h...

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created	[InstanceEdit:8985092] Shamovsky, Veronica, 2017-04-11
dbId	8985144
displayName	Gel filtration experiments using extracts from IFN-treated h...
literatureReference	[LiteratureReference:8985090] The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases [LiteratureReference:8985083] Identification of the substrate-binding sites of 2'-5'-oligoadenylate synthetase [LiteratureReference:1015642] Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon
modified	[InstanceEdit:9015149] Shamovsky, Veronica, 2017-08-08
schemaClass	Summation
text	Gel filtration experiments using extracts from IFN-treated human HeLa and Daudi cells showed that 2',5'-oligoadenylate (2-5A) synthetase (OAS2, p69) exists as a dimer of 160 kDa (Marie I et al. 1990). Biochemical and mutational studies demonstrated that dimerization of OAS2 protein is required for its enzyme activity (Sarkar SN et al. 1999). Further, photo affinity cross-linking and peptide mapping to study the substrate binding sites in OAS2 have suggested that OAS2 is active only as a dimer because it catalyzes the joining of the acceptor substrate bound to one subunit to the donor substrate bound to the other subunit (Sarkar SN et al. 2002).

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