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Literature summary for 3.2.1.1 extracted from
- Cloning and characterization of cold-adapted alpha-amylase from antarctic Arthrobacter agilis (2017), Appl. Biochem. Biotechnol., 181, 1048-1059 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | activates 91.2% at 5 mM | Arthrobacter agilis |  |
| FeCl3 | activates 152.3% at 1 mM | Arthrobacter agilis | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene amy, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Arthrobacter agilis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ammonium persulfate | 54% inhibition at 5 mM | Arthrobacter agilis | |
| Ca2+ | 7% inhibition at 1 mM | Arthrobacter agilis | |
| Co2+ | 63% inhibition at 1 mM | Arthrobacter agilis | |
| Mg2+ | 22% inhibition at 1 mM | Arthrobacter agilis | |
| SDS | 39% inhibition at 10% | Arthrobacter agilis | |
| Triton X-100 | 45% inhibition at 10% | Arthrobacter agilis | |
| Urea | 64.5% inhibition at 1% | Arthrobacter agilis | |
| Zn2+ | 36% inhibition at 1 mM | Arthrobacter agilis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe3+ | activates 152% at 1 mM | Arthrobacter agilis | |
| K+ | activates 10% at 1 mM | Arthrobacter agilis | |
| Na+ | activates 15% at 1 mM | Arthrobacter agilis | |
| PMSF | activates 12% at 1 mM | Arthrobacter agilis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Arthrobacter agilis | alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units | ? | - |
? | |
| additional information | Arthrobacter agilis PAMC 27388 | alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arthrobacter agilis | A0A1D9CEW3 | isolated from seawater in Antarctica King George Island (South Shetland Islands) | - |
| Arthrobacter agilis PAMC 27388 | A0A1D9CEW3 | isolated from seawater in Antarctica King George Island (South Shetland Islands) | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Arthrobacter agilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 27.96 | - |
purified recombinant enzyme, pH 7.0, 25°C, substrate soluble starch | Arthrobacter agilis |
| 60 | - |
purified recombinant enzyme, pH 3.0, 25°C, substrate soluble starch | Arthrobacter agilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydrolyzed starch + H2O | 0.5-2.0% soluble starch | Arthrobacter agilis | maltose | - |
? | |
| hydrolyzed starch + H2O | 0.5-2.0% soluble starch | Arthrobacter agilis PAMC 27388 | maltose | - |
? | |
| maltotetraose + H2O | - |
Arthrobacter agilis | 2 maltose | - |
? | |
| maltotetraose + H2O | - |
Arthrobacter agilis PAMC 27388 | 2 maltose | - |
? | |
| maltotriose + H2O | - |
Arthrobacter agilis | maltose + D-glucose | - |
? | |
| maltotriose + H2O | - |
Arthrobacter agilis PAMC 27388 | maltose + D-glucose | - |
? | |
| additional information | alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units | Arthrobacter agilis | ? | - |
? | |
| additional information | recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product | Arthrobacter agilis | ? | - |
? | |
| additional information | alpha-amylases are endo-acting enzymes that randomly cleave the 1,4-alpha-D-glucosidic linkages between adjacent glucose units in linear amylose chains. As a result, they generate dextrins and smaller polymers composed of glucose units | Arthrobacter agilis PAMC 27388 | ? | - |
? | |
| additional information | recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product | Arthrobacter agilis PAMC 27388 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 80000, recombinant His6-tagged enzyme, SDS-PAGE, x * 79610, sequence calculation | Arthrobacter agilis |
| More | the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902) | Arthrobacter agilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 1,4-alpha-D-glucan-glucanohydrolase | - |
Arthrobacter agilis |
| Amy | - |
Arthrobacter agilis |
| cold-adapted alpha-amylase | - |
Arthrobacter agilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
recombinant enzyme | Arthrobacter agilis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | specific activities of 32, 30, 29, and 30 U/mg at 30, 40, 50, and 60°C, respectively | Arthrobacter agilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 60 | recombinant enzyme, highly stable at | Arthrobacter agilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
recombinant enzyme | Arthrobacter agilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 2 | 10 | the alpha-amylase exhibits optimal activity of 60 U/mg at pH 3.0 and retains high specific activity of 50 U/mg at pH 2.0. Enzyme activity declines sharply at pH values above pH 3.0, retaining only about 48-27 U/mg between pH 4.0 and 10.0, respectively | Arthrobacter agilis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | recombinant enzyme, retains over 60% of its activity between pH 4.0 and pH 9.0 after incubation for 24 h | Arthrobacter agilis |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Arthrobacter agilis | sequence calculation | - |
9.11 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the alpha-amylase has an alpha-1,4-glucan-maltose-1-phosphate maltosyltransferase domain (IPR021828) (aa 20-206) and a GH13 family domain (aa 199-574) of glycoside hydrolase (IPR015902) | Arthrobacter agilis |
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