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Literature summary for 3.2.1.1 extracted from
- Characterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose (2016), Insect Biochem. Mol. Biol., 74, 1-11 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3) | Callosobruchus chinensis |
| sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21 Star (DE3) in inclusion bodies | Tribolium castaneum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acarbose | enzyme binding and docking study | Callosobruchus chinensis |  |
| acarbose | enzyme binding and docking study | Tribolium castaneum | |
| wheat amylase inhibitor | a proteinaceous inhibitor | Callosobruchus chinensis | |
| wheat amylase inhibitor | a proteinaceous inhibitor | Tribolium castaneum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetic analysis | Callosobruchus chinensis | |
| additional information | - |
additional information | Michaelis-Menten kinetic analysis | Tribolium castaneum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme contains a signal peptide | Callosobruchus chinensis | - |
- |
| extracellular | the enzyme contains a signal peptide | Tribolium castaneum | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | Callosobruchus chinensis | - |
D-glucose + maltose + maltotriose | - |
? | |
| starch + H2O | Tribolium castaneum | - |
maltose + maltotriose + maltotetraose | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Callosobruchus chinensis | A0A168VCK5 | i.e. Pachymerus chinensis | - |
| Tribolium castaneum | P09107 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography | Callosobruchus chinensis |
| recombinant solubilized and refolded His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography | Tribolium castaneum |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21 Star (DE3) inclusion bodies using solubilization of the enzyme protein in denaturing buffer containing 20 mM Tris, pH 8.5, 8 M urea, 100 mM NaCl, 1 mM 2-mercaptoethanol, followed by a on-column refolding method | Tribolium castaneum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylopectin + H2O | - |
Tribolium castaneum | ? | - |
? | |
| amylopectin + H2O | preferred substrate | Callosobruchus chinensis | ? | - |
? | |
| starch + H2O | - |
Callosobruchus chinensis | D-glucose + maltose + maltotriose | - |
? | |
| starch + H2O | - |
Tribolium castaneum | maltose + maltotriose + maltotetraose | - |
? | |
| starch + H2O | preferred substrate | Tribolium castaneum | maltose + maltotriose + maltotetraose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional enzyme structure modelling | Callosobruchus chinensis |
| More | three-dimensional enzyme structure modelling | Tribolium castaneum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CcAmy | - |
Callosobruchus chinensis |
| TcAmy | - |
Tribolium castaneum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
recombinant enzyme | Tribolium castaneum |
| 50 | - |
recombinant enzyme | Callosobruchus chinensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.92 | - |
starch | pH 5.0, 37°C, recombinant enzyme | Callosobruchus chinensis | |
| 1.1 | - |
amylopectin | pH 5.0, 37°C, recombinant enzyme | Callosobruchus chinensis | |
| 1.13 | - |
starch | pH 5.0, 37°C, recombinant enzyme | Tribolium castaneum | |
| 1.4 | - |
amylopectin | pH 5.0, 37°C, recombinant enzyme | Tribolium castaneum | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Callosobruchus chinensis |
| 5 | - |
recombinant enzyme | Tribolium castaneum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic tree of coleopteran alpha-amylases | Callosobruchus chinensis |
| evolution | phylogenetic tree of coleopteran alpha-amylases | Tribolium castaneum |
| additional information | homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview | Callosobruchus chinensis |
| additional information | homology modeling and molecular docking of alpha-amylase from Callosobruchus chinensis and comparison to the alpha-amylase from Tribolium castaneum showing structural differences between these two enzymes, overview | Tribolium castaneum |
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