EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
---|
2.7.11.18 | -999 |
- |
more |
in the presence of wortmannin |
640640 |
2.7.11.18 | -999 |
- |
more |
kinetic constants for enzymes from various sources with different myosin light chains as substrates |
640645 |
2.7.11.18 | -999 |
- |
more |
kinetics of myosin light chain kinase activation of smooth muscle myosin in an in vitro model system, kinetic modelling, overview. The dissociation of MLCK from phosphorylated smooth muscle myosin is rate-limiting and that the rate of the phosphorylation step is faster than this dissociation rate. Association to smooth muscle myosin is much faster than to smooth muscle myosin. The probability of MLCK interacting with unphosphorylated versus smooth muscle myosin is 55-460 times greater |
740060 |
2.7.11.18 | -999 |
- |
more |
Michaelis-Menten kinetics, kinetic scheme of the mathematical model considers interactions among Ca2+, calmodulin and MLCK, and the well-known 4-state actomyosin latch bridge model, whereby a link between them is accomplished by the conservation relation of all species of MLCK, detailed overview |
688705 |
2.7.11.18 | -999 |
- |
more |
steady-state kinetic parameters of MLCK toward 4 different substrates: the 2-headed heavy meromyosin (HMM) soluble subfragments of both smooth muscle myosin II and non-muscle myosin IIB, each containing their respective smooth or non-muscle regulatory light chains, and the 2 types of free regulatory light chains. MLCK has an about 2fold higher kcat for both smooth muscle myosin II substrates compared with non-muscle myosin IIB substrates, whereas Km values are very similar |
740266 |
2.7.11.18 | 0.000002 |
- |
Calmodulin |
30°C, pH 6.8 |
640623 |
2.7.11.18 | 0.000002 |
- |
Calmodulin |
30°C, pH 7.5 |
640628 |
2.7.11.18 | 0.0025 |
- |
[non-muscle heavy meromyosin IIB] |
pH 7.6, 25°C |
740266 |
2.7.11.18 | 0.0026 |
- |
[smooth muscle heavy meromyosin] |
pH 7.6, 25°C |
740266 |
2.7.11.18 | 0.004 |
- |
Dictyostelium myosin |
22°C, pH 7.5 |
491266 |