EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
3.5.4.6 | -999 |
- |
more |
- |
209681, 209682, 209686, 209689, 209690, 209691, 209693, 209694 |
3.5.4.6 | -999 |
- |
more |
at pH 7.0 the reaction catalysed by AMP-deaminase from human preterm placenta follows a well depicted sigmoid-shaped kinetic profile, with a half-saturation constant (S0.5) value of about 9.2 mM. Phosphate hardly influences the kinetic profile diminishing the S0.5 constant value slightly to 8.1 mM. Addition into the medium of 1 mM adenine nucleotide, ADP or ATP, transforms the sigmoid-shaped profile of the control kinetic curve into a hyperbolic one, diminishing simultaneously the value of the S0.5 constant from 9.2 mM to 2.4 mM, respectively. Kinetic analysis, overview |
720641 |
3.5.4.6 | -999 |
- |
more |
kinetics |
654807 |
3.5.4.6 | -999 |
- |
more |
kinetics, stearyl-CoA influences the reaction kinetics |
656779 |
3.5.4.6 | 0.223 |
- |
AMP |
pH 6.0, 40°C |
756756 |
3.5.4.6 | 0.27 |
- |
AMP |
pH 6.0, temperature not specified in the publication |
755821 |
3.5.4.6 | 0.4 |
- |
AMP |
crude enzyme extract, pH 6.5, 20°C |
654859 |
3.5.4.6 | 0.54 |
- |
AMP |
- |
209712 |
3.5.4.6 | 0.6 |
- |
AMP |
- |
209713 |
3.5.4.6 | 0.6 |
- |
AMP |
imidazole-eluted purified enzyme, pH 6.5, 20°C |
654859 |