EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.1.1.56 | 0.036 |
- |
GTP |
isolated methyltransferase domain |
485467 |
| 2.1.1.56 | 0.05 |
- |
G(5')pppR-RNA |
mutant enzyme F679L, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C |
706721 |
| 2.1.1.56 | 0.07221 |
- |
S-adenosyl-L-methionine |
at pH 7.3 and 25°C |
758535 |
| 2.1.1.56 | 0.074 |
- |
G(5')pppR-RNA |
mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C |
706721 |
| 2.1.1.56 | 0.085 |
- |
G(5')pppG |
intact mRNA capping enzyme |
485467 |
| 2.1.1.56 | 0.1 |
- |
GpppA |
- |
674439 |
| 2.1.1.56 | 0.101 |
- |
G(5')pppG |
isolated methyltransferase domain |
485467 |
| 2.1.1.56 | 0.143 |
- |
G(5')pppR-RNA |
mutant enzyme F679N, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C |
706721 |
| 2.1.1.56 | 0.176 |
- |
G(5')pppR-RNA |
mutant enzyme F679I, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C |
706721 |
| 2.1.1.56 | 0.18 |
- |
S-adenosyl-L-methionine |
pH 7.5, 20°C, Michaelis constants for S-adenosyl-methionine (AdoMet) in both reactions are about 10fold lower than for their respective RNA substrates, suggesting that the rate-limiting steps in methylase reactions are associated with RNA templates |
721099 |
