EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.2.1.6 | -999 |
- |
more |
activity is dependent on the ionic strength of the buffer and diminishes considerably (approximately 80%) when assayed in buffers with less than 100 mM concentrations. At concentrations higher than 100 mM the activity levels are quite similar (tested up to 500 mM) |
733241 |
| 2.2.1.6 | -999 |
- |
more |
binding kinetics of Mg2+ and thiamine diphosphate with wild-type enzyme and mutant enzymes, overview |
733987 |
| 2.2.1.6 | -999 |
- |
more |
cofactor affinities of wild-type and mutant enzymes, overview |
672866 |
| 2.2.1.6 | -999 |
- |
more |
kinetics |
671290, 671854, 673626 |
| 2.2.1.6 | -999 |
- |
more |
kinetics of isozymes |
673213 |
| 2.2.1.6 | -999 |
- |
more |
kinetics of wild-type and mutant enzymes |
674354 |
| 2.2.1.6 | -999 |
- |
more |
kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model |
672368 |
| 2.2.1.6 | -999 |
- |
more |
Michaelis-Menten kinetics and optimal reaction conditions, overview |
733744 |
| 2.2.1.6 | -999 |
- |
more |
Michaelis-Menten steady-state kinetic analysis, overview |
733241 |
| 2.2.1.6 | -999 |
- |
more |
non-hyperbolic substrate-saturation curve, involving interaction between the active sites of the dimer |
395902 |
