General Stability | Organism |
---|---|
the apo-form of the enzyme is marginally stable | Equus caballus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | binding constants and thermodynamics of Ca2+ and Mg2+ binding, overview | Equus caballus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required, strong temperature dependences of apparent affinities to Ca2+ due to low thermal stability of the apoform, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site, Ca2+-binding sites are generally able to bind Mg2+., overview | Equus caballus | |
Mg2+ | required, strong temperature dependences of apparent affinities to Mg2+ due to low thermal stability of the apoform and relatively high unfavorable enthalpies of Mg2+ association, the primary Mg2+ site of the enzyme is different from its Ca2+-binding site. The Ca2+/Mg2+ selectivity of Mg2+-site of EQL is below an order of magnitude. The enzyme exhibits a distinct Mg2+-specific site, probably arising as an adaptation to the extracellular environment, overview | Equus caballus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Equus caballus | - |
- |
- |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25.3 | - |
loss of 50% activity | Equus caballus |