EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.4.1.2 | -999 |
- |
more |
cofactor kinetics, overview |
724249 |
| 1.4.1.2 | -999 |
- |
more |
cofactor kinetics, overview. Even without the heterotropic antenna responsible for allosteric regulation in mammalian enzymes, the GDH is emphatically still allosteric. The Eadie-Hofstee plot for NAD+ is strongly non-linear.Att pH 9.0 there is almost total positive co-operativity with glutamate, with a Hill coefficient close to the theoretical maximum of 6 for a hexamer |
724249 |
| 1.4.1.2 | -999 |
- |
more |
dissociation constants of wild-type and mutant enzymes for different coenzymes, overview |
711875 |
| 1.4.1.2 | -999 |
- |
more |
enzyme kinetics of wild-tyype and mutant enzymes with NADPH, overview |
724888 |
| 1.4.1.2 | -999 |
- |
more |
kinetics of recombinant wild-type and mutant enzymes with NADH/NAD+ and NADPH/NADP+, overview |
724970 |
| 1.4.1.2 | -999 |
- |
more |
no significant changes in Km values between groups treated with alkalized extract from the tuber of Corydalis ternata or protopine and control groups |
673480 |
| 1.4.1.2 | -999 |
- |
more |
the enzyme shows positive cooperativity towards 2-oxoglutarate and NADH, and Michaelis-Menten type kinetics with ammonium chloride in the absence of catalytic activator L-aspartate. L-aspartate effect on enzyme kinetics, overview |
711526 |
| 1.4.1.2 | -999 |
- |
more |
wild-type Vmax: 23.71 (pH 7), 35.16 (pH 9) |
697928 |
| 1.4.1.2 | 0.000011 |
- |
L-glutamate |
pH 9.0, 40°C, recombinant enzyme |
724935 |
| 1.4.1.2 | 0.000025 |
- |
L-glutamate |
pH 9.0, 40°C, recombinant enzyme in presence of DMSO |
724935 |
