EC Number   |
Reaction |
Reference |
|---|
   2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
active domain between residues 520 and 545, comprises both activities, the ATPase and guanylyltransferase activity |
643483 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
active site |
-, 643482, 643491 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
active site Lys177 |
643492 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
active site Lys190 |
-, 643491 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
ATP/GTP-binding-site motif A, residues 379-386 |
-, 643493 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
conserved KXDG-motif |
643484, 643490, 643492 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
GTP:RNA GTase, the GTase component of MimiCE, catalyzes a reversible two-step ping-pong reaction. The first step entails nucleophilic attack of the enzyme at the a phosphorus of GTP to form a covalent enzyme-(lysyl-N)-GMP intermediate plus pyrophosphate. In the second step, the beta-phosphate of 50 diphosphate-terminated RNA attacks the enzyme-GMP intermediate to form the GpppRNA cap and expel the lysine nucleophile |
695159 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
guanylyltransferase domain: residues 211-597 |
643486 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
Lys294 is located in the active site in a KXDG-conserved motif |
643484 |
| 2.7.7.50 | GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA |
magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation |
721658 |
