EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
   2.4.1.5 | -999 |
- |
more |
- |
489263, 489266 |
| 2.4.1.5 | -999 |
- |
more |
DSase has a high affinity for dextran as first substrate with Kd of 18 nM, kinetic analysis of 27 MHz quartz crystal microbalance, QCM, plate-immobilized enzyme, overview |
720352 |
| 2.4.1.5 | -999 |
- |
more |
effect of temperature on KM-value |
489264 |
| 2.4.1.5 | -999 |
- |
more |
enzyme deactivation follows fi rst order rate kinetics |
719584 |
| 2.4.1.5 | -999 |
- |
more |
kinetic analysis of the low-molecular-weight products D-glucose, D-fructose, leucrose and isomaltodextrins formed during the synthesis of dextran by B-512FMC dextransucrase, overview |
703051 |
| 2.4.1.5 | -999 |
- |
more |
kinetic modeling of fed-batch isomaltose production in a bi-enzymic system with immobolized enzymes, overview |
678832 |
| 2.4.1.5 | -999 |
- |
more |
kinetics analysis of continuously truncated enzymes with sucrose and maltose as the substrate |
756615 |
| 2.4.1.5 | -999 |
- |
more |
Km for dextran T-500 is 1.57 mg/ml in glucosyl transfer from dextran T-500 to maltose. The Km-value for dextran T-500 is 0.019 mg/ml in hydrolysis of dextran T-500 |
489277 |
| 2.4.1.5 | -999 |
- |
more |
Michaelis-Menten kinetics |
736230, 737067, 737154 |
| 2.4.1.5 | -999 |
- |
more |
rDSRC39-2 shows Michaelis-Menten-type kinetics |
718682 |
