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Literature summary for 3.2.1.1 extracted from
- 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.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | effects of several commercial detergent products on the activities of the enzyme mutants, overview | Bacillus sp. (in: Bacteria) |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain M15 | Bacillus sp. (in: Bacteria) |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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
| General Stability | Organism |
|---|---|
| wild-type andmutant enzymes exhibit sensitivity towards GdnHCl-induced denaturation | Bacillus sp. (in: Bacteria) |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 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) | |
| SDS | - |
Bacillus sp. (in: Bacteria) |  |
| Triton X-100 | - |
Bacillus sp. (in: Bacteria) | |
| Tween-20 | - |
Bacillus sp. (in: Bacteria) | |
| Tween-80 | - |
Bacillus sp. (in: Bacteria) | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of recombinant mutant enzymes, overiew | Bacillus sp. (in: Bacteria) |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Bacillus sp. (in: Bacteria) | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
x * 54000, recombinant wild-type enzyme, SDS-PAGE | Bacillus sp. (in: Bacteria) |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. (in: Bacteria) | - |
- |
- |
| Bacillus sp. (in: Bacteria) TS-23 | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| the enzyme mutants are more stable to H2O2 than the wild-type enzyme, overview | Bacillus sp. (in: Bacteria) |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 142.2 | - |
purified recombinant mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
| 145.4 | - |
purified recombinant mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
| 158.9 | - |
purified recombinant mutant BACDELTANC/DELTARS, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
| 179.6 | - |
purified recombinant mutant BACDELTANC/M231L, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
| 193.3 | - |
purified recombinant mutant BACDELTANC, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| raw starch + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| raw starch + H2O | - |
Bacillus sp. (in: Bacteria) TS-23 | ? | - |
? | |
| soluble starch + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| soluble starch + H2O | - |
Bacillus sp. (in: Bacteria) TS-23 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 54000, recombinant wild-type enzyme, SDS-PAGE | Bacillus sp. (in: Bacteria) |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at, substrate raw starch | Bacillus sp. (in: Bacteria) |
| 60 | - |
assay at, substrate soluble starch | Bacillus sp. (in: Bacteria) |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 139.1 | - |
soluble starch | mutant BACDELTANC/DELTARS/M231L/DELTAC31, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) | |
| 141.3 | - |
soluble starch | mutant BACDELTANC/DELTARS/M231L, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) | |
| 147.5 | - |
soluble starch | mutant BACDELTANC/M231L, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) | |
| 156.8 | - |
soluble starch | mutant BACDELTANC/DELTARS, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) | |
| 168.5 | - |
soluble starch | mutant BACDELTANC, pH 8.0, 60°C | Bacillus sp. (in: Bacteria) |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Bacillus sp. (in: Bacteria) |
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