EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
1.1.1.49 | -999 |
- |
more |
- |
286819, 286982, 286984, 286986, 286987, 286988, 286991, 286992, 286996, 286998, 287001, 655712 |
1.1.1.49 | -999 |
- |
more |
hyperbolic kinetics versus D-glucose 6-phosphate |
722212 |
1.1.1.49 | -999 |
- |
more |
kinetics |
657147 |
1.1.1.49 | -999 |
- |
more |
kinetics and thermodynamics, rapid equilibrium random bi bi kinetic model |
655736 |
1.1.1.49 | -999 |
- |
more |
kinetics, kinetic mechanism analysis, ternary-complex mechanism, overview |
674379 |
1.1.1.49 | -999 |
- |
more |
Michaelis-Menten kinetics |
723340 |
1.1.1.49 | -999 |
- |
more |
ping pong bi bi kinetic mechanism |
673156 |
1.1.1.49 | -999 |
- |
more |
steady-state kinetics of wild-type and mutant enzymes |
672382, 673944 |
1.1.1.49 | -999 |
- |
more |
the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface |
722577 |
1.1.1.49 | -999 |
- |
more |
thermodynamics, steady-state kinetics |
657284 |