EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    1.2.1.79 | -999 |
- |
more |
enzyme does not obey Michaelis-Menten kinetics |
288054 |
| 1.2.1.79 | -999 |
- |
more |
Michaelis-Menten kinetics |
741822, 762707 |
| 1.2.1.79 | -999 |
- |
more |
steady-state kinetic analysis. Pre-steady-state kinetics show burst kinetics for NADPH formation in SSADH, indicating that the rate-limiting step is associated with steps that occur after the hydride transfer. Detection of burst kinetics of NADPH production by pre-steady-state analysis indicates that the rate-limiting step of the AbSSADH reaction occurs after the hydride transfer step |
763015 |
| 1.2.1.79 | -999 |
- |
more |
the Km-value of succinate semialdehyde estimated to be far less than 0.05 mM |
725523 |
| 1.2.1.79 | 0.001 |
- |
succinate semialdehyde |
pH 6.5, 70°C, cofactor NAD+ |
722211 |
| 1.2.1.79 | 0.003 |
- |
Succinic semialdehyde |
steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C |
724115 |
| 1.2.1.79 | 0.00395 |
- |
succinate semialdehyde |
recombinant enzyme, pH 7.0, 30°C |
741822 |
| 1.2.1.79 | 0.004 |
- |
succinate semialdehyde |
pH 6.5, 70°C, cofactor NADP+ |
722211 |
| 1.2.1.79 | 0.0078 |
- |
succinate semialdehyde |
pH 8.5, 22°C |
690736 |
| 1.2.1.79 | 0.0092 |
- |
NADP+ |
steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C |
724115 |
