Any feedback?
Literature summary extracted from
- Cloning and characterization of cold-adapted alpha-amylase from antarctic Arthrobacter agilis (2017), Appl. Biochem. Biotechnol., 181, 1048-1059 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | 2-mercaptoethanol | activates 91.2% at 5 mM | Arthrobacter agilis |  |
| 3.2.1.1 | FeCl3 | activates 152.3% at 1 mM | Arthrobacter agilis | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | 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
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | ammonium persulfate | 54% inhibition at 5 mM | Arthrobacter agilis | |
| 3.2.1.1 | Ca2+ | 7% inhibition at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | Co2+ | 63% inhibition at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | Mg2+ | 22% inhibition at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | SDS | 39% inhibition at 10% | Arthrobacter agilis | |
| 3.2.1.1 | Triton X-100 | 45% inhibition at 10% | Arthrobacter agilis | |
| 3.2.1.1 | Urea | 64.5% inhibition at 1% | Arthrobacter agilis | |
| 3.2.1.1 | Zn2+ | 36% inhibition at 1 mM | Arthrobacter agilis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | Fe3+ | activates 152% at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | K+ | activates 10% at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | Na+ | activates 15% at 1 mM | Arthrobacter agilis | |
| 3.2.1.1 | PMSF | activates 12% at 1 mM | Arthrobacter agilis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | 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 | ? | - |
? | |
| 3.2.1.1 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Arthrobacter agilis | A0A1D9CEW3 | isolated from seawater in Antarctica King George Island (South Shetland Islands) | - |
| 3.2.1.1 | Arthrobacter agilis PAMC 27388 | A0A1D9CEW3 | isolated from seawater in Antarctica King George Island (South Shetland Islands) | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis | Arthrobacter agilis |
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 | 27.96 | - |
purified recombinant enzyme, pH 7.0, 25°C, substrate soluble starch | Arthrobacter agilis |
| 3.2.1.1 | 60 | - |
purified recombinant enzyme, pH 3.0, 25°C, substrate soluble starch | Arthrobacter agilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | hydrolyzed starch + H2O | 0.5-2.0% soluble starch | Arthrobacter agilis | maltose | - |
? | |
| 3.2.1.1 | hydrolyzed starch + H2O | 0.5-2.0% soluble starch | Arthrobacter agilis PAMC 27388 | maltose | - |
? | |
| 3.2.1.1 | maltotetraose + H2O | - |
Arthrobacter agilis | 2 maltose | - |
? | |
| 3.2.1.1 | maltotetraose + H2O | - |
Arthrobacter agilis PAMC 27388 | 2 maltose | - |
? | |
| 3.2.1.1 | maltotriose + H2O | - |
Arthrobacter agilis | maltose + D-glucose | - |
? | |
| 3.2.1.1 | maltotriose + H2O | - |
Arthrobacter agilis PAMC 27388 | maltose + D-glucose | - |
? | |
| 3.2.1.1 | 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 | ? | - |
? | |
| 3.2.1.1 | additional information | recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product | Arthrobacter agilis | ? | - |
? | |
| 3.2.1.1 | 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 | ? | - |
? | |
| 3.2.1.1 | additional information | recombinant Arthrobacter agilis alpha-amylase hydrolyzed starch, maltotetraose, and maltotriose, produces maltose as the major end product | Arthrobacter agilis PAMC 27388 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | ? | x * 80000, recombinant His6-tagged enzyme, SDS-PAGE, x * 79610, sequence calculation | Arthrobacter agilis |
| 3.2.1.1 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | 1,4-alpha-D-glucan-glucanohydrolase | - |
Arthrobacter agilis |
| 3.2.1.1 | Amy | - |
Arthrobacter agilis |
| 3.2.1.1 | cold-adapted alpha-amylase | - |
Arthrobacter agilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 30 | - |
recombinant enzyme | Arthrobacter agilis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 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]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 10 | 60 | recombinant enzyme, highly stable at | Arthrobacter agilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 3 | - |
recombinant enzyme | Arthrobacter agilis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 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
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 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
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.2.1.1 | Arthrobacter agilis | sequence calculation | - |
9.11 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
