EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.1.1.72 | -999 |
- |
more |
detailed kinetics for diverse substrate duplexes and methylation sites |
660031 |
| 2.1.1.72 | -999 |
- |
more |
detailed kinetics, enzyme shows a simple kinetic behaviour towards a 20mer duplex DNA, random bi bi mechanism |
659200 |
| 2.1.1.72 | -999 |
- |
more |
detailed steady-state and pre-steady-state kinetics for different methylation sites |
659301 |
| 2.1.1.72 | -999 |
- |
more |
kinetics, ordered bi bi kinetic mechanism, cooperative binding of 2 molecules of enzyme per DNA is required for activity |
659303 |
| 2.1.1.72 | -999 |
- |
more |
Km-values for oligonucleotide substrates containing the native or modified recognition site: 5.3-12.9 nM |
485570 |
| 2.1.1.72 | -999 |
- |
more |
Km-values fpr 14-mers and various substituted duplexes |
485578 |
| 2.1.1.72 | -999 |
- |
more |
pre-steady-state and steady-state kinetics, reaction kinetics with diverse DNA duplex substrates, role of individual elements of the recognition site, kinetic reaction scheme assuming that the enzyme is isomerized into a catalytically active form, overview |
659905 |
| 2.1.1.72 | -999 |
- |
more |
quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes |
659715 |
| 2.1.1.72 | -999 |
- |
more |
steady-state and pre-steady-state kinetics, single turnover methylation kinetics |
659268 |
| 2.1.1.72 | -999 |
- |
more |
steady-state kinetics, kinetic mechanism, thermodynamics |
659422 |
