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Literature summary extracted from

  • Wu, X.; Wang, Y.; Tong, B.; Chen, X.; Chen, J.
    Purification and biochemical characterization of a thermostable and acid-stable alpha-amylase from Bacillus licheniformis B4-423 (2018), Int. J. Biol. Macromol., 109, 329-337 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.1 Tween 20 8.9% inhibition at 20%, 9.2% activation at 10% Bacillus licheniformis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 DNA and amino acid sequence determination and analysis, sequence comparisons Bacillus licheniformis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 2-mercaptoethanol 37.6% inhibition at 1 mM, 43.7% at 5 mM Bacillus licheniformis
3.2.1.1 ascorbate 28.4% inhibition at 5 mM, 34.9% at 10 mM Bacillus licheniformis
3.2.1.1 Ba2+ 5.3% inhibition at 1 mM, 11.1% at 5 mM Bacillus licheniformis
3.2.1.1 Co2+ 11.1% inhibition at 1 mM, 89.4% at 5 mM Bacillus licheniformis
3.2.1.1 Cu2+ complete inhibition at 1-5 mM Bacillus licheniformis
3.2.1.1 Dimethyl formamide 38.2% inhibition at 1 mM, 72.0% at 5 mM Bacillus licheniformis
3.2.1.1 DTNB 55.2% inhibition at 5 mM Bacillus licheniformis
3.2.1.1 DTT 61.9% inhibition at 1 mM, 84.8% at 5 mM Bacillus licheniformis
3.2.1.1 EDTA 19.3% inhibition at 5 mM Bacillus licheniformis
3.2.1.1 Fe2+ 94.1% inhibition at 1 mM, complete inhibition at 5 mM Bacillus licheniformis
3.2.1.1 Fe3+ complete inhibition at 1-5 mM Bacillus licheniformis
3.2.1.1 H2O2 82.3% inhibition at 0.5%, 43.7% at 5 mM Bacillus licheniformis
3.2.1.1 Mn2+ 7.1% inhibition at 1 mM, 22.4% at 5 mM Bacillus licheniformis
3.2.1.1 additional information no effect by 5-10 mM of urea and glycerol, poor effects by 0.5-1% sodium tetraborate Bacillus licheniformis
3.2.1.1 Pb2+ 74.5% inhibition at 1 mM, complete inhibition at 5 mM Bacillus licheniformis
3.2.1.1 PMSF 36.5% inhibition at 1mM, 53.7% at 5 mM Bacillus licheniformis
3.2.1.1 SDS 14.9% inhibition at 2% Bacillus licheniformis
3.2.1.1 Sodium citrate 23.1% inhibition at 5 mM Bacillus licheniformis
3.2.1.1 Triton X-100 12.4% inhibition at 10% Bacillus licheniformis
3.2.1.1 Tween 20 8.9% inhibition at 20%, 9.2% activation at 10% Bacillus licheniformis
3.2.1.1 Tween 80 8.3% inhibition at 20% Bacillus licheniformis
3.2.1.1 Zn2+ 59.2% inhibition at 1 mM, 94.3% at 5 mM Bacillus licheniformis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 additional information the enzyme shows Ca2+-independency, no effect by Ca2+ at 1-5 mM. Poor effects by 1-5 mM of Na+, K+, and Mg2+ Bacillus licheniformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 58000
-
 about, gel filtration Bacillus licheniformis

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.2.1.1 2-propanol loss of 83% activity at 10% 2-propanol after 30 min at room temperature Bacillus licheniformis
3.2.1.1 Acetone loss of 15% activity at 20% acetone after 30 min at room temperature Bacillus licheniformis
3.2.1.1 Butanol loss of 89% activity at 10% butanol after 30 min at room temperature Bacillus licheniformis
3.2.1.1 additional information the enzyme activity is poorly affected by 10-20% of methanol, ethanol, chloroform, isoamylalcohol, and hexane after 30 min at room temperature Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus licheniformis
-
 isolated from a hot spring
-
3.2.1.1 Bacillus licheniformis B4-423
-
 isolated from a hot spring
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 native extracellular enzyme 8.34fold by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography Bacillus licheniformis

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 2902.26
-
 purified enzyme, pH 5.0, 100°C, substrate starch Bacillus licheniformis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 starch + H2O 1% w/v starch solution Bacillus licheniformis ?
-
 ?
3.2.1.1 starch + H2O 1% w/v starch solution Bacillus licheniformis B4-423 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 monomer 1 * 58000, SDS-PAGE Bacillus licheniformis
3.2.1.1 More comparison of primary and secondary enzyme structure Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 100
-
-
 Bacillus licheniformis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.1 20 150 20% of maximal activity at 20°C, 30% at 50°C, 65% at 60°C, 75% at 80°C and 150°C, 90% at 90°C and 110-130°C, profile overview Bacillus licheniformis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.1 20 70 purified native enzyme, 10 min, completely stable at Bacillus licheniformis
3.2.1.1 80
-
 purified native enzyme, 10 min, 70% activity remaining Bacillus licheniformis
3.2.1.1 90
-
 purified native enzyme, 10 min, 10% activity remaining Bacillus licheniformis
3.2.1.1 100
-
 purified native enzyme, 10 min, no activity remaining Bacillus licheniformis

pH Optimum

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

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.1 4 10 about 15% of maximal activity at pH 4.0, 75% at pH 8.0, and 70% at pH 10.0, profile overview Bacillus licheniformis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.1 4 10 purified native enzyme, highly stable at Bacillus licheniformis