EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.7.4 | -999 |
- |
more |
- |
643252 |
2.7.7.4 | -999 |
- |
more |
Michaelis-Menten kinetics, substrate kinetic mechanism of ATP sulfurylase: rapid equilibrium rate equations describe ordered sequential and random sequential kinetic mechanisms, overview |
739744 |
2.7.7.4 | -999 |
- |
more |
Michealis-Menten kinetics, overview |
739483 |
2.7.7.4 | -999 |
- |
more |
steady-state kinetic analysis of wild-type and mutant enzymes, overview |
738608 |
2.7.7.4 | -999 |
- |
more |
the Michaelis constants are 1.55-2.29 mM for corrosive and 2.93-3.13 mM for intestinal bacteria strains |
760241 |
2.7.7.4 | -999 |
- |
more |
the reaction does not strictly follow Michaelis-Menten kinetics |
643261 |
2.7.7.4 | 0.0003 |
- |
adenosine 5'-phosphosulfate |
pH 8.0, 30°C |
641208, 643268 |
2.7.7.4 | 0.0004 |
- |
adenylylsulfate |
pH 8.0, 30°C, wild-type enzyme |
662282 |
2.7.7.4 | 0.0005 |
- |
adenylylsulfate |
pH 8.0, 30°C, truncated mutant enzyme del396-573 |
662282 |
2.7.7.4 | 0.00053 |
- |
adenosine 5'-phosphosulfate |
pH 8.0, 30°C, cytosolic enzyme |
643282 |