EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference  |
|---|
   2.1.1.228 | 0.00047 |
- |
guanine37 in tRNACys |
recombinant enzyme, pH 7.3, 37°C |
737226 |
| 2.1.1.228 | 0.0012 |
- |
guanine37 in tRNALeu(CAG) |
pH and temperature not specified in the publication |
755697 |
| 2.1.1.228 | 0.0018 |
- |
S-adenosyl-L-methionine |
pH and temperature not specified in the publication |
755697 |
| 2.1.1.228 | -999 |
- |
more |
Michaelis-Menten kinetic analysis |
756161 |
| 2.1.1.228 | -999 |
- |
more |
binding kinetics of TrmD ligands |
757409 |
| 2.1.1.228 | -999 |
- |
more |
pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays |
757582 |
| 2.1.1.228 | -999 |
- |
more |
kinetics and thermodynamics analysis, overview. Steady-state kinetics with S-adenosyl-L-methionine (SAM) and tRNALeu(GAG) show that PaTrmD catalyzes the two-substrate reaction by way of a ternary-complex, while isothermal titration calorimetry revealed that SAM and tRNALeu(GAG) bind to PaTrmD independently, each with a dissociation constant of 0.014 mM |
758329 |
| 2.1.1.228 | 0.0008 |
- |
guanine37 in tRNALeu(GAG) |
pH 7.5, 37°C, recombinant enzyme |
758329 |
| 2.1.1.228 | 0.003 |
- |
S-adenosyl-L-methionine |
pH 7.5, 37°C, recombinant enzyme |
758329 |
