EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.7.1.26 | -999 |
- |
more |
bi-substrate enzyme kinetics of the recombinant DELTA(1-182)CaFADS module |
737357 |
| 2.7.1.26 | -999 |
- |
more |
Michaelis-Menten kinetics and modeling, cooperativity model, pre-steady-state kinetics/pre-steady-state stopped-flow kinetics and dissociation constants, overview. Isothermal titration calorimetry, and Gibbs free energy flow for the interaction of HsRFK with substrates and products. Thermodynamics modulates the ligand binding landscape of HsRFK. Cooperativity coefficients, ANP and FLV ligands cooperate in their binding to HsRFK |
759167 |
| 2.7.1.26 | -999 |
- |
more |
Michaelis-Menten model and thermodynamic profiles of recombinant wild-type and mutant enzymes, overview |
737771 |
| 2.7.1.26 | -999 |
- |
more |
Michaelis-Menten steady-state kinetic study. While Km ATP values increase with the ADP concentration, kcat values remain constant. The high affinity for the ADP product inhibitor considerably increases the estimated error for KmATP. Association and dissociation kinetics of flavin ligands to the RFK module are measured by flavin fluorescence changes, stopped-flow kinetics. Pre-steady-state kinetic analysis of the binding of flavins to the RFK module of CaFADS, thermodynamic diagram for the RFK-ligand interactions. Adenine and flavin nucleotide ligands cooperate in their binding to the RFK module. Detailed kinetic analysis, overview |
760159 |
| 2.7.1.26 | -999 |
- |
more |
steady-state kinetic analysis of wild-type and mutant enzymes |
737678 |
| 2.7.1.26 | 0.0000103 |
- |
riboflavin |
bifunctional enzyme AtFMN/FHy |
680633 |
| 2.7.1.26 | 0.000021 |
- |
ATP |
ATP in form of MgATP2- |
641249 |
| 2.7.1.26 | 0.000021 |
- |
ATP |
pH 8.5, 30°C |
641249 |
| 2.7.1.26 | 0.00012 |
- |
riboflavin |
pH 8.5, 30°C |
641249 |
| 2.7.1.26 | 0.0002 |
- |
ATP |
bifunctional enzyme AtFMN/FHy |
680633 |
