EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.5.1.3 | -999 |
- |
more |
- |
392208, 392212, 392224, 392227, 392229, 392236, 392237, 392238, 392239, 392240, 392241, 392242, 392243, 392247, 392248, 392249, 392254, 392263, 392265, 392290 |
| 1.5.1.3 | -999 |
- |
more |
analysis of steady-state kinetics at pH 9.5 |
671846 |
| 1.5.1.3 | -999 |
- |
more |
buffer and salt conditions significantly alter the Km-values for the substrates |
392281 |
| 1.5.1.3 | -999 |
- |
more |
enzyme activity decreases with increasing pressure. The Km values for dihydrofolate and NADPH are slightly higher at 200 MPa than at atmospheric pressure. The hydride transfer step is insensitive to pressure, while the dissociation constants of substrates and cofactors increase with pressure |
685386 |
| 1.5.1.3 | -999 |
- |
more |
kinetic behavior of the wild-type enzyme ecDHFR and enzyme mutants D27S, Y100F, and D27S/Y100F across an extended pH range, including pH 9.0. Competitive hydrogen to deuterium and hydrogen to tritium kinetic isotope effects (KIEs) on the second-order rate constant (kcat/Km) are measured for wild-type and mutant ecDHFR variants to assess the intrinsic KIE on the catalyzed hydride transfer. Presteady-state, Michaelis-Menten, and single-turnover kinetics |
743678 |
| 1.5.1.3 | -999 |
- |
more |
kinetics by non-tight binding Michaelis-Menten model |
765513 |
| 1.5.1.3 | -999 |
- |
more |
Km of enzymes with decreased binding of folate and antagonists and of drug-sensitive enzymes |
392208 |
| 1.5.1.3 | -999 |
- |
more |
Michaelis-Menten kinetics |
742057, 742438, 742491, 743569 |
| 1.5.1.3 | -999 |
- |
more |
Michaelis-Menten steady-state kinetics |
741613, 743741 |
| 1.5.1.3 | -999 |
- |
more |
molecular dynamics and spectroscopic analysis of the enzyme in transition state based on residues Tyr100 and Tyr111, overview |
701696 |
