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Literature summary for 3.2.1.1 extracted from
- Biochemical, structural and functional diversity between two digestive alpha-amylases from Helicoverpa armigera (2015), Biochim. Biophys. Acta, 1850, 1719-1728 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene GH13Amy-1, DNA and amino acid sequence determination and analysis, isozyme structure comparisons, recombinant expression in Pichia pastoris | Helicoverpa armigera |
| gene GH13Amy-2, DNA and amino acid sequence determination and analysis, isozyme structure comparisons, recombinant expression in Pichia pastoris | Helicoverpa armigera |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acarbose | - |
Helicoverpa armigera |  |
| additional information | isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview; isozymes HaAmy1 and HaAmy2 are inhibited to the same magnitude by the synthetic amylase inhibitor (acarbose), while wheat amylase inhibitor shows about 2 and 6fold higher inhibition of isozyme HaAmy1 compared to isozyme HaAmy2 at pH 7.0 and pH 11.0, respectively. Amylase-inhibitor docking and molecular dynamic simulations, overview | Helicoverpa armigera | |
| wheat amylase inhibitor | from Triticum aestivum; from Triticum aestivum | Helicoverpa armigera |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km for starch is 2.0 mg/ml and for amylpectin 1.1 mg/ml for isozyme HaAmy2 | Helicoverpa armigera | |
| additional information | - |
additional information | Km for starch is 9.2 mg/ml and for amylpectin 1.3 mg/ml for isozyme HaAmy1 | Helicoverpa armigera |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | Helicoverpa armigera | - |
D-glucose + maltose + maltotriose | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Helicoverpa armigera | B1NLD3 | - |
- |
| Helicoverpa armigera | B1NLD4 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylopectin + H2O | - |
Helicoverpa armigera | ? | - |
? | |
| starch + H2O | - |
Helicoverpa armigera | D-glucose + maltose + maltotriose | - |
? | |
| starch + H2O | 1% potato starch solution | Helicoverpa armigera | D-glucose + maltose + maltotriose | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GH13Amy-1 | - |
Helicoverpa armigera |
| GH13Amy-2 | - |
Helicoverpa armigera |
| HaAmy1 | - |
Helicoverpa armigera |
| HaAmy2 | - |
Helicoverpa armigera |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Helicoverpa armigera |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 80 | activity range, profile overview | Helicoverpa armigera |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 70 | activity of purified recombinant HaAmy1 when carried out under standard assay conditions is retained at 50°C incubation while decreased by 70% when incubated at 70°C | Helicoverpa armigera |
| 50 | 70 | activity of purified recombinant HaAmy2 when carried out under standard assay conditions is reduced by 15% at 50°C incubation while decreased by 70% when incubated at 70°C | Helicoverpa armigera |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.13 | - |
amylopectin | isozyme HaAmy2, pH 7.0, 37°C | Helicoverpa armigera | |
| 0.19 | - |
starch | isozyme HaAmy2, pH 7.0, 37°C | Helicoverpa armigera | |
| 0.29 | - |
amylopectin | isozyme HaAmy1, pH 7.0, 37°C | Helicoverpa armigera | |
| 0.67 | - |
starch | isozyme HaAmy1, pH 7.0, 37°C | Helicoverpa armigera | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Helicoverpa armigera |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 11 | purified recombinant isozyme HaAmy1 is completely stable at, isozymes HaAmy1 and HaAmy2 show 10% and 5% increase in the amylase activity at pH 9.0 and pH 5.0, respectively | Helicoverpa armigera |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | three-dimensional structure homology modeling of isozymes HaAmy1 and HaAmy2 | Helicoverpa armigera |
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