EC Number   |
Natural Substrates |
|---|
   2.1.1.56 | more |
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation |
| 2.1.1.56 | more |
the enzyme is responsible for guanine-N7 methylation of recapped mRNAs |
| 2.1.1.56 | S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] |
- |
| 2.1.1.56 | S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] |
the enzyme methylates the guanosine cap on the N-7 position to create the cap structure, m7G(5)ppp(5)X |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
- |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
the presence of the small one is required for methylase activity, the large subunit bears functional domains for binding of the small subunit and for methylase activity |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
guanylyltransferase and RNA-triphosphatase are located on the large subunit |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
one of a series of three reactions in capping of vaccinia virus mRNA catalyzed by one enzyme, which is a heterodimer: no methylase activity with one of the subunits alone |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
in infected BHK cells |
| 2.1.1.56 | S-adenosyl-L-methionine + G(5')pppR-RNA |
associated with mRNA-guanylyltransferase |
