Table 2.
Steady-State Kinetic Parameters for Wild-type Fmsl and the N195A and D94N Enzymesa
| substrate | kinetic parameter | Fms1d | N195A | D94N |
|---|---|---|---|---|
| N1-acetylspermineb | kcat (s-1)c | 15.1 ± 0.4 | 8.1 ± 0.2 | 9.7 ± 0.2 |
| kcat/Kamine (mM-1 s-1)c | 1400 ± 200 | 78 ± 13 | 320 ± 50 | |
| Kamine (μM)c | 10.9 ± 1.8 | 104 ± 14 | 30 ± 5 | |
| kcat/KO2 (mM-1 s-1)e | 358 ± 20 | 405 ± 72 | 100 ± 14 | |
| KO2 (μM)e | 43.6 ± 2.3 | 20 ± 3 | 97 ± 14 | |
| sperminef | kcat (s-1)c | 39.0 ± 1.5 | 4.9 ± 0.2 | 2.0 ± 0.3 |
| kcat/Kamine (mM-1 s-1)c | 330 ± 60 | 38.5 ± 8.3 | 4.1 ± 1.0 | |
| Kamine (μM)c | 118 ± 25 | 127 ± 27 | 320 ± 88 | |
| kcat/KO2 (mM-1 s-1)g | 428 ± 77 | 327 ± 67 | 104 ± 36 | |
| KO2 (μM)g | 91 ± 16 | 15 ± 3 | 192 ± 60 |
Conditions: 25 °C.
Determined at pH 9.0.
Determined by varying the concentration of the amine at 1.2 mM oxygen.
From ref. (13).
Determined by varying the concentration of oxygen at 20 mM N1-acetylspermine.
Determined at pH 9.35.
Determined by varying the concentration of oxygen at 20 mM spermine.