EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    3.5.1.5 | -999 |
- |
more |
kinetic analysis of enzyme immobilized on acrylonitrile copolymer membranes chemically modified by different methods. KM-value of enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2 is equal to that of free enzyme |
670117 |
| 3.5.1.5 | -999 |
- |
more |
reaction kinetics and thermodynamics, overview |
733568 |
| 3.5.1.5 | -999 |
- |
more |
sigmoid curve at low urea concentration (below 0.1 mM). In the presence of glycerol or PEG (preservatives), the sigmoid pattern changes to a rectangular hyperbola, and urea hydrolysis is consistent with Michaelis-Menten kinetics. Based on the kinetics of urease in the presence of the preservatives, the two forms of urease i.e., (alpha beta)3 and (alpha beta)6 may well exist in Helicobacter pylori. The hyperbolic kinetics adopted by the dissociated form of urease may allow for maximal urea assimilation by Helicobacter pylori under acidic conditions and at low urea concentration |
712722 |
| 3.5.1.5 | -999 |
- |
more |
steady-state kinetics analysis |
733467, 733784 |
| 3.5.1.5 | -999 |
- |
Urea |
a combined temperature-pH study of urease kinetics is performed at eight pHs between 5.0 and 8.3 in noninteracting biological buffers (MES and HEPES), at each pH at five temperatures between 15°C and 35°C. The analysis of the determined kinetic parameters KM and vmax shows that even though both the thermodynamic and activation parameters of the urease reaction are little pH-dependent |
754437 |
| 3.5.1.5 | 0.0195 |
- |
Urea |
- |
695706 |
| 3.5.1.5 | 0.0195 |
- |
Urea |
35°C, pH 4.5 |
695706 |
| 3.5.1.5 | 0.071 |
- |
Urea |
pH 7.0, 25°C, soluble enzyme |
752526 |
| 3.5.1.5 | 0.11 |
- |
Urea |
pH 8.4, temperature not specified in the publication |
712785 |
| 3.5.1.5 | 0.12 |
- |
Urea |
- |
209157, 687256 |
