EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.3.4 | -999 |
- |
more |
comparisons of wild-type and mutant enzyme kinetics, overview |
739402 |
2.7.3.4 | -999 |
- |
more |
steady-state kinetic analysis, overview. Analysis of quaternary structure and cooperativity in ligand-binding by ITC: absence of inter-subunit cooperativity in forming the PsTKTSAC |
738077 |
2.7.3.4 | 0.082 |
- |
Taurocyamine |
mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.1 |
- |
N-taurocyamine |
pH 8.0, 25°C |
642485 |
2.7.3.4 | 0.14 |
- |
Taurocyamine |
mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.153 |
- |
Taurocyamine |
mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.184 |
- |
Taurocyamine |
mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.205 |
- |
Taurocyamine |
mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.217 |
- |
Taurocyamine |
mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
721715 |
2.7.3.4 | 0.269 |
- |
Taurocyamine |
isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25°C |
722083 |