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Literature summary for 3.2.1.17 extracted from

  • Permyakov, S.; Khokhlova, T.; Uversky, V.; Permyakov, E.
    Analysis of Ca2+/Mg2+ selectivity in alpha-lactalbumin and Ca2+-binding lysozyme reveals a distinct Mg2+-specific site in lysozyme (2010), Proteins, 78, 2609-2624.
    View publication on PubMed

General Stability

General Stability Organism
the apo-form of the enzyme is marginally stable Equus caballus

KM Value [mM]

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

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

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25.3
-
loss of 50% activity Equus caballus