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Literature summary extracted from

  • Duy, C.; Fitter, J.
    Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics (2005), J. Biol. Chem., 280, 37360-37365.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information thermodynamics and kinetics Bacillus subtilis
3.2.1.1 additional information
-
 additional information thermodynamics and kinetics Sus scrofa
3.2.1.1 additional information
-
 additional information thermodynamics and kinetics Bacillus licheniformis
3.2.1.1 additional information
-
 additional information thermodynamics and kinetics Bacillus amyloliquefaciens
3.2.1.1 additional information
-
 additional information thermodynamics and kinetics Aspergillus oryzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ increases the thermostability of the enzyme, five Ca2+ ions per enzyme molecule Bacillus licheniformis
3.2.1.1 Ca2+ increases the thermostability of the enzyme, four Ca2+ ions per enzyme molecule Bacillus amyloliquefaciens
3.2.1.1 Ca2+ increases the thermostability of the enzyme, one Ca2+ ion per enzyme molecule Sus scrofa
3.2.1.1 Ca2+ increases the thermostability of the enzyme, three Ca2+ ions per enzyme molecule Bacillus subtilis
3.2.1.1 Ca2+ increases the thermostability of the enzyme, two Ca2+ ions per enzyme molecule Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Aspergillus oryzae
-
-
-
3.2.1.1 Bacillus amyloliquefaciens
-
-
-
3.2.1.1 Bacillus licheniformis
-
-
-
3.2.1.1 Bacillus subtilis
-
-
-
3.2.1.1 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 commercial preparation
-
 Bacillus subtilis
-
3.2.1.1 commercial preparation
-
 Bacillus licheniformis
-
3.2.1.1 commercial preparation
-
 Bacillus amyloliquefaciens
-
3.2.1.1 commercial preparation
-
 Aspergillus oryzae
-
3.2.1.1 commercial preparation pancreatic alpha-amylase Sus scrofa
-
3.2.1.1 pancreas
-
 Sus scrofa
-

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme Bacillus subtilis
3.2.1.1 additional information
-
 analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme Sus scrofa
3.2.1.1 additional information
-
 analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme Bacillus licheniformis
3.2.1.1 additional information
-
 analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme Bacillus amyloliquefaciens
3.2.1.1 additional information
-
 analysis of thermostability of irreversibly unfolding alpha-amylases, unfolding kinetics, Ca2+ increases the thermostability of the enzyme Aspergillus oryzae