EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    4.2.1.1 | -999 |
- |
more |
- |
33543, 33551 |
| 4.2.1.1 | -999 |
- |
more |
during the second catalytic stage, the zinc-bound 18O-labeled hydroxide is protonated, forming H2 18O, which is then released into solution, 18O-exchange kinetic analysis, overview |
746623 |
| 4.2.1.1 | -999 |
- |
more |
influence of buffer composition and pH on the Km-value |
33548 |
| 4.2.1.1 | -999 |
- |
more |
influence of pH and buffer composition on Km-values |
33561 |
| 4.2.1.1 | -999 |
- |
more |
influence of pH-value and buffer composition on Km-value on native enzyme and on an activated derivative with modified thiol groups |
33570 |
| 4.2.1.1 | -999 |
- |
more |
intrinsic second order kinetic constant kcat/KM for the CO2 hydration reaction catalyzed by the immobilized CA |
747013 |
| 4.2.1.1 | -999 |
- |
more |
kinetic and thermodynamic analysis, molecular modelling, overview |
746912 |
| 4.2.1.1 | -999 |
- |
more |
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+ |
727848 |
| 4.2.1.1 | -999 |
- |
more |
kinetics |
747974 |
| 4.2.1.1 | -999 |
- |
more |
kinetics of 4-nitrophenyl acetate hydrolysis reaction |
748131 |
