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Literature summary extracted from

  • Ghalanbor, Z.; Ghaemi, N.; Marashi, S.A.; Amanlou, M.; Habibi-Rezaei, M.; Khajeh, K.; Ranjbar, B.
    Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity (2008), Protein Pept. Lett., 15, 212-214.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 Tris starch-hydrolyzing activity in presence of Tris of different concentrations, pH 7.4, 37°C Bacillus licheniformis

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O soluble starch, 2000000 Dalton, only soluble at temperatures close to 100°C, in phosphate buffer, pH 7.4, assay at 37°C Bacillus licheniformis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 Bacillus licheniformis alpha-amylase
-
 Bacillus licheniformis
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 37
-
 assay at Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 additional information
-
 Bacillus licheniformis is routinely used as a model thermostable amylase, since starch as the substrate is only soluble at tempertures closed to 100°C Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 7.4
-
 assay at Bacillus licheniformis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.1 13
-
 Tris determined with Lineweaver-Burk plot, competitive inhibition, pH 7.4, 37°C, docking simulations show that Tris binds deep inside the active site of the enzyme Bacillus licheniformis