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Literature summary extracted from

  • Fitter, J.; Haber-Pohlmeier, S.
    Structural stability and unfolding properties of thermostable bacterial alpha-amylases: a comparative study of homologous enzymes (2004), Biochemistry, 43, 9589-9599.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.2.1.1 unfolding kinetics, unfolding induced by guanidine hydrochloride Bacillus amyloliquefaciens
3.2.1.1 unfolding kinetics, unfolding induced by guanidine hydrochloride Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus amyloliquefaciens
-
-
-
3.2.1.1 Bacillus licheniformis P06278
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.1 commercial preparation
-
 Bacillus amyloliquefaciens
-
3.2.1.1 commercial preparation
-
 Bacillus licheniformis
-

Subunits

EC Number Subunits Comment Organism
3.2.1.1 additional information three-dimensional structure analysis of intact and unfolded enzyme Bacillus amyloliquefaciens
3.2.1.1 additional information three-dimensional structure analysis of intact and unfolded enzyme Bacillus licheniformis

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 BAA
-
 Bacillus amyloliquefaciens
3.2.1.1 BLA
-
 Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 thermodynamics, overview Bacillus amyloliquefaciens
3.2.1.1 additional information
-
 thermodynamics, overview Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 thermal unfolding kinetics and thermal stability, overview Bacillus amyloliquefaciens
3.2.1.1 additional information
-
 thermal unfolding kinetics and thermal stability, overview Bacillus licheniformis