EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.7.1.20 | -999 |
- |
more |
kinetic data of nucleosides and nucleoside analogs |
641088 |
| 2.7.1.20 | -999 |
- |
more |
kinetic study |
641086, 641092, 641094 |
| 2.7.1.20 | -999 |
- |
more |
pH and Mg/ATP ratio-dependent Km |
641089 |
| 2.7.1.20 | -999 |
- |
more |
removal of residues 17 to 28 from the N-terminal end of the protein leads to an increase in the Km for adenosine. Removal of the first 10 residues from the C-terminal end causes a 5fold increase in the Km for ATP |
641110 |
| 2.7.1.20 | 0.0000081 |
- |
adenosine |
with ATP as cosubstrate, at 27°C in 50 mM Tris buffer (pH 7.4) containing 5 mM MgCl2, 50 mM KCl, and 0.2 mM dithiothreitol |
721633 |
| 2.7.1.20 | 0.00002 |
- |
adenosine |
recombinant isozymes AK-S and AK-L, pH 7.5, 37°C |
661642 |
| 2.7.1.20 | 0.000041 |
- |
adenosine |
pH 7.6, 37°C |
687787 |
| 2.7.1.20 | 0.00007 |
- |
adenosine |
pH 7.5, 37ºC |
641104 |
| 2.7.1.20 | 0.00012 |
- |
adenosine |
pH 7.2, 37ºC |
641092 |
| 2.7.1.20 | 0.00015 |
0.0005 |
adenosine |
- |
641075, 641077, 641089, 641091 |
