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Literature summary extracted from

  • Chi, M.C.; Chen, Y.H.; Wu, T.J.; Lo, H.F.; Lin, L.L.
    Engineering of a truncated alpha-amylase of Bacillus sp. strain TS-23 for the simultaneous improvement of thermal and oxidative stabilities (2010), J. Biosci. Bioeng., 109, 531-538.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.1 additional information effects of several commercial detergent products on the activities of the enzyme mutants, overview Bacillus sp. (in: Bacteria)

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.1 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15 Bacillus sp. (in: Bacteria)

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.1 M231L construction of a thermostable variant BACDELTANC/DELTARS derived from the truncated alpha-amylase BACDELTANC, introduction of mutation M231L for enhancing the resistance towards chemical oxidation, and site-directed mutagenesis of the 483th codon in the gene to stop codon, resulting in the mutants BACDELTANC/DELTARS/M231L/DELTAC31. Mutants BACDELTANC/DELTARS/M231L and BACDELTANC/DELTARS/M231L/DELTAC31 are very similar to BACDELTANC in terms of specific activity, kinetic parameters, pH-activity profile, and the hydrolysis of raw starch, but the engineered enzymes show an increased half-life at 70°C Bacillus sp. (in: Bacteria)

General Stability

EC Number General Stability Organism
3.2.1.1 wild-type andmutant enzymes exhibit sensitivity towards GdnHCl-induced denaturation Bacillus sp. (in: Bacteria)

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.1 additional information wild-type and mutant enzymes exhibit sensitivity towards GdnHCl-induced denaturation, effects of several commercial detergent products on the activities of the enzyme mutants, overview Bacillus sp. (in: Bacteria)
3.2.1.1 SDS
-
 Bacillus sp. (in: Bacteria)
3.2.1.1 Triton X-100
-
 Bacillus sp. (in: Bacteria)
3.2.1.1 Tween-20
-
 Bacillus sp. (in: Bacteria)
3.2.1.1 Tween-80
-
 Bacillus sp. (in: Bacteria)

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.1 additional information
-
 additional information kinetics of recombinant mutant enzymes, overiew Bacillus sp. (in: Bacteria)

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.1 Ca2+ required Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.1 54000
-
 x * 54000, recombinant wild-type enzyme, SDS-PAGE Bacillus sp. (in: Bacteria)

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.1 Bacillus sp. (in: Bacteria)
-
-
-
3.2.1.1 Bacillus sp. (in: Bacteria) TS-23
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.2.1.1 the enzyme mutants are more stable to H2O2 than the wild-type enzyme, overview Bacillus sp. (in: Bacteria)

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.1 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.1 142.2
-
 purified recombinant mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 145.4
-
 purified recombinant mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 158.9
-
 purified recombinant mutant BACDELTANC/DELTARS, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 179.6
-
 purified recombinant mutant BACDELTANC/M231L, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 193.3
-
 purified recombinant mutant BACDELTANC, pH 8.0, 60°C Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.1 raw starch + H2O
-
 Bacillus sp. (in: Bacteria) ?
-
 ?
3.2.1.1 raw starch + H2O
-
 Bacillus sp. (in: Bacteria) TS-23 ?
-
 ?
3.2.1.1 soluble starch + H2O
-
 Bacillus sp. (in: Bacteria) ?
-
 ?
3.2.1.1 soluble starch + H2O
-
 Bacillus sp. (in: Bacteria) TS-23 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.1 ? x * 54000, recombinant wild-type enzyme, SDS-PAGE Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.1 50
-
 assay at, substrate raw starch Bacillus sp. (in: Bacteria)
3.2.1.1 60
-
 assay at, substrate soluble starch Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.1 139.1
-
 soluble starch mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 141.3
-
 soluble starch mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 147.5
-
 soluble starch mutant BACDELTANC/M231L, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 156.8
-
 soluble starch mutant BACDELTANC/DELTARS, pH 8.0, 60°C Bacillus sp. (in: Bacteria)
3.2.1.1 168.5
-
 soluble starch mutant BACDELTANC, pH 8.0, 60°C Bacillus sp. (in: Bacteria)

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.1 8
-
 assay at Bacillus sp. (in: Bacteria)