EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    5.4.3.5 | -999 |
- |
more |
kinetic isotope effects analysis using isotope-labeled DL-ornithine-3,3,4,4,5,5-d6 revealing a diminished Dkcat/Km of 2.5 relative to a Dkcat of 7.6, suggesting slow release of the substrate from the active site. Kinetic isotope effects are not observed on the he rate constant associated with Co-C bond homolysis as this step is likely gated by the formation of the external aldimine. Stopped-flow kinetics, and Michaelis-Menten steady-state kinetics |
747073 |
| 5.4.3.5 | -999 |
- |
more |
Michaelis-Menten kinetics |
727131 |
| 5.4.3.5 | -999 |
- |
more |
pre-steady-state and stedy-state kinetics of wild-type and mutant enzymes |
727036 |
| 5.4.3.5 | -999 |
- |
more |
steady-state and pre-steady-state kinetics |
748182 |
| 5.4.3.5 | -999 |
- |
more |
steady-state kinetics of wild-type enzyme and beta-subunit mutants, enzyme dynamics and C-Co bond homolysis in single-turnover stopped-flow kinetics |
747738 |
| 5.4.3.5 | 0.029 |
- |
D-ornithine |
pH 8.5, 25°C, recombinant beta-subunit mutant S162A |
747193 |
| 5.4.3.5 | 0.03 |
- |
D-ornithine |
recombinant His-tagged mutant E338A, pH 7.5, 30°C |
727036 |
| 5.4.3.5 | 0.031 |
- |
D-ornithine |
pH 8.5, 25°C, recombinant beta-subunit mutant Y187F |
747193 |
| 5.4.3.5 | 0.043 |
- |
D-ornithine |
pH 8.5, 25°C, recombinant wild-type enzyme |
747193 |
| 5.4.3.5 | 0.043 |
- |
D-ornithine |
recombinant His-tagged mutant E338D, pH 7.5, 30°C |
727036 |
