EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    4.3.2.2 | -999 |
- |
more |
Michaelis-Menten kinetics |
729717 |
| 4.3.2.2 | -999 |
- |
more |
non-linear dependence of the activities on the substrate ratios due to competitive binding. The enzyme does not follow simple Michaelis-Menten kinetics, kinetic analysis of wild-type and mutant enzymes, overview. Wild-type enzyme and mutant R426H appear to have equivalent cooperative binding on both substrates, while mutant R303C demonstrates no cooperativity |
729296 |
| 4.3.2.2 | -999 |
- |
more |
pH-dependence of Km-value |
34461 |
| 4.3.2.2 | -999 |
- |
more |
the enzyme shows cooperativity and does not follow simple Michaelis-Menten kinetics, kinetic analysis, overview |
729218 |
| 4.3.2.2 | -999 |
- |
more |
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview |
691116 |
| 4.3.2.2 | 0.0003 |
- |
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide |
pH 7.0, 25°C, mutant S290A |
695003 |
| 4.3.2.2 | 0.0007 |
- |
phosphoribosylsuccinyl-aminoimidazole carboxamide |
recombinant His-tagged mutant R426H, pH 7.4, 25°C |
729296 |
| 4.3.2.2 | 0.0008 |
- |
2'-deoxy-succino-AMP |
- |
1541 |
| 4.3.2.2 | 0.001 |
- |
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide |
- |
34449 |
| 4.3.2.2 | 0.0012 |
- |
N6-(1,2-dicarboxyethyl)AMP |
- |
34451 |
