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Literature summary extracted from

  • Liu, Y.; Shen, W.; Shi, G.Y.; Wang, Z.X.
    Role of the calcium-binding residues Asp231, Asp233, and Asp438 in alpha-amylase of Bacillus amyloliquefaciens as revealed by mutational analysis (2010), Curr. Microbiol., 60, 162-166.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 D231N the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH Bacillus amyloliquefaciens
3.2.1.1 D233N the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively Bacillus amyloliquefaciens
3.2.1.1 D438G the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH Bacillus amyloliquefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 25.1
-
 starch mutant enzyme D233N Bacillus amyloliquefaciens
3.2.1.1 157
-
 starch mutant enzyme D231N Bacillus amyloliquefaciens
3.2.1.1 161.7
-
 starch mutant enzyme D438G Bacillus amyloliquefaciens
3.2.1.1 167.6
-
 starch wild type enzyme Bacillus amyloliquefaciens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ the Ca2+-binding residue Asp233 affects significantly the alpha-amylase specific activity Bacillus amyloliquefaciens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 58000
-
 SDS-PAGE Bacillus amyloliquefaciens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.1 starch + H2O Bacillus amyloliquefaciens
-
 malto-oligosaccharides
-
 ?
3.2.1.1 starch + H2O Bacillus amyloliquefaciens CICIM B2125
-
 malto-oligosaccharides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus amyloliquefaciens P00692
-
-
3.2.1.1 Bacillus amyloliquefaciens CICIM B2125 P00692
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O
-
 Bacillus amyloliquefaciens malto-oligosaccharides
-
 ?
3.2.1.1 starch + H2O
-
 Bacillus amyloliquefaciens CICIM B2125 malto-oligosaccharides
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.1 AmyQ
-
 Bacillus amyloliquefaciens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 50 75 in presence of 5 mM Ca2+, the optimum temperature of AmyQ is between 50 and 75°C Bacillus amyloliquefaciens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 60
-
 AmyQ remains stable at 60°C for 30 min Bacillus amyloliquefaciens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 5 7
-
 Bacillus amyloliquefaciens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 5 9.5
-
 Bacillus amyloliquefaciens