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Literature summary for 3.2.1.1 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
Search for more literature for 3.2.1.1

General Stability

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

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
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-
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Bacillus licheniformis P06278
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Bacillus amyloliquefaciens
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commercial preparation
-
 Bacillus licheniformis
-

Subunits

Subunits Comment Organism
More three-dimensional structure analysis of intact and unfolded enzyme Bacillus amyloliquefaciens
More three-dimensional structure analysis of intact and unfolded enzyme Bacillus licheniformis

Synonyms

Synonyms Comment Organism
BAA
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 Bacillus amyloliquefaciens
BLA
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 Bacillus licheniformis

Temperature Optimum [°C]

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

Temperature Stability [°C]

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