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Literature summary extracted from

  • Najafi, M.F.; Deobagkar, D.; Deobagkar, D.
    Purification and characterization of an extracellular alpha-amylase from Bacillus subtilis AX20 (2005), Protein Expr. Purif., 41, 349-354.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 Ag+
-
Bacillus subtilis
3.2.1.1 Cu2+
-
Bacillus subtilis
3.2.1.1 Hg2+
-
Bacillus subtilis
3.2.1.1 additional information mo inhibition by EDTA or EGTA Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.1 extracellular
-
Bacillus subtilis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 additional information the enzyme shows no requirement for metals Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 79000
-
2 * 79000, SDS-PAGE Bacillus subtilis
3.2.1.1 139400
-
gel filtration Bacillus subtilis

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 subtilis
-
maltose + D-glucose
-
?
3.2.1.1 starch + H2O Bacillus subtilis AX20
-
maltose + D-glucose
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus subtilis
-
isolated from soil
-
3.2.1.1 Bacillus subtilis AX20
-
isolated from soil
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.1 glycoprotein
-
Bacillus subtilis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 native extracellular enzyme 37.5fold to homogeneity by ammonium sulfate fractionation, ion exchange and starch affinity chromatography, and gel filtration Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
3.2.1.1 (alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose + (alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose endo mode of action Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.1 4133
-
purified enzyme Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O
-
Bacillus subtilis maltose + D-glucose
-
?
3.2.1.1 starch + H2O raw starch from corn and soluble starch, endo mode of action Bacillus subtilis maltose + D-glucose 25% maltose, 75% glucose ?
3.2.1.1 starch + H2O
-
Bacillus subtilis AX20 maltose + D-glucose
-
?
3.2.1.1 starch + H2O raw starch from corn and soluble starch, endo mode of action Bacillus subtilis AX20 maltose + D-glucose 25% maltose, 75% glucose ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 dimer 2 * 79000, SDS-PAGE Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 55
-
-
Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 50
-
30 min, purified enzyme, stable Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 6
-
-
Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 5 9 purified enzyme, stable, 24 h at 4°C Bacillus subtilis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.1 Bacillus subtilis isoelectric focusing
-
7