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Literature summary for 3.2.1.1 extracted from
- Isolation and characterisation of a novel alpha-amylase from the extreme haloarchaeon Haloterrigena turkmenica (2016), Int. J. Biol. Macromol., 92, 174-184 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | poor effects by PEG 1500, PEG 3350, and PEG 8000 | Haloterrigena turkmenica | |
| Triton X-100 | activates 21.2% at 1.0% v/v | Haloterrigena turkmenica |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene htur2110, sequence comparisons | Haloterrigena turkmenica |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate | CHAPS, 39.2% inhibition at 1% v/v | Haloterrigena turkmenica | |
| Tween 20 | 89.4% inhibition at 1% v/v | Haloterrigena turkmenica | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Haloterrigena turkmenica | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory | Haloterrigena turkmenica | |
| NaCl | activates, optimal at 2 M for highest enzyme activity, profile overview | Haloterrigena turkmenica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 54000 | - |
gel filtration | Haloterrigena turkmenica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| starch + H2O | Haloterrigena turkmenica | - |
? | - |
? | |
| starch + H2O | Haloterrigena turkmenica ATCC 51198 | - |
? | - |
? | |
| starch + H2O | Haloterrigena turkmenica NCIMB 13204 | - |
? | - |
? | |
| starch + H2O | Haloterrigena turkmenica DSM 5511 | - |
? | - |
? | |
| starch + H2O | Haloterrigena turkmenica VKM B-1734 | - |
? | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| Acetone | at 20% v/v, loss of 96.8% activity | Haloterrigena turkmenica |
| chloroform | at 20% v/v, activates by 5.7% activity | Haloterrigena turkmenica |
| Ethanol | at 20% v/v, loss of 88.3% activity | Haloterrigena turkmenica |
| Methanol | at 20% v/v, loss of 89.8% activity | Haloterrigena turkmenica |
| n-Butanol | at 20% v/v, loss of 70.8% activity | Haloterrigena turkmenica |
| n-hexane | at 20% v/v, activates by 9.5% activity | Haloterrigena turkmenica |
| n-propanol | at 20% v/v, loss of 87.5% activity | Haloterrigena turkmenica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloterrigena turkmenica | D2RTP2 | catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus | - |
| Haloterrigena turkmenica ATCC 51198 | D2RTP2 | catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus | - |
| Haloterrigena turkmenica DSM 5511 | D2RTP2 | catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus | - |
| Haloterrigena turkmenica NCIMB 13204 | D2RTP2 | catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus | - |
| Haloterrigena turkmenica VKM B-1734 | D2RTP2 | catalytic region of the alpha-amylase; i.e. Halococcus turkmenicus | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from culture supernatant 33.1fold by centrifugation at 55000 rpm, dialysis, ultrafiltration, anion exchange chromatography, dialysis, and gel filtration | Haloterrigena turkmenica |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | culture is grown in medium containing potato starch at 0.2% w/v | Haloterrigena turkmenica | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
one enzyme unit is defined as the amount of enzyme that hydrolyses 1 mg of starch in 1 min | Haloterrigena turkmenica |
| 79.8 | - |
purified enzyme, pH 8.5, 55°C | Haloterrigena turkmenica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan | Haloterrigena turkmenica | ? | - |
? | |
| additional information | the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan | Haloterrigena turkmenica ATCC 51198 | ? | - |
? | |
| additional information | the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan | Haloterrigena turkmenica NCIMB 13204 | ? | - |
? | |
| additional information | the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan | Haloterrigena turkmenica DSM 5511 | ? | - |
? | |
| additional information | the enzyme is highly active on starch (highest activity) and high molecular weight maltodextrins (97.5% activity). The enzyme is inactive towards alpha-cyclodextrin and beta-cyclodextrin, and it does not display debranching activity on alpha-1,6-glycosidic linkages, showing no action towards pullulan | Haloterrigena turkmenica VKM B-1734 | ? | - |
? | |
| potato starch + H2O | 1% w/v potato starch | Haloterrigena turkmenica | ? | - |
? | |
| potato starch + H2O | 1% w/v potato starch | Haloterrigena turkmenica ATCC 51198 | ? | - |
? | |
| potato starch + H2O | 1% w/v potato starch | Haloterrigena turkmenica NCIMB 13204 | ? | - |
? | |
| potato starch + H2O | 1% w/v potato starch | Haloterrigena turkmenica DSM 5511 | ? | - |
? | |
| potato starch + H2O | 1% w/v potato starch | Haloterrigena turkmenica VKM B-1734 | ? | - |
? | |
| starch + H2O | - |
Haloterrigena turkmenica | ? | - |
? | |
| starch + H2O | - |
Haloterrigena turkmenica ATCC 51198 | ? | - |
? | |
| starch + H2O | - |
Haloterrigena turkmenica NCIMB 13204 | ? | - |
? | |
| starch + H2O | - |
Haloterrigena turkmenica DSM 5511 | ? | - |
? | |
| starch + H2O | - |
Haloterrigena turkmenica VKM B-1734 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 66000, SDS-PAGE, 1 * 49800, catalytic region of the enzyme, SDS-PAGE | Haloterrigena turkmenica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmyA | - |
Haloterrigena turkmenica |
| endo-1,4-alpha-D-glucan glucanohydrolase | - |
Haloterrigena turkmenica |
| htur2110 | - |
Haloterrigena turkmenica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
- |
Haloterrigena turkmenica |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 65 | activity range, profile overview. 55% of maximal activity at 60°C | Haloterrigena turkmenica |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 55 | purified enzyme, 2 M NaCl, pH 8.5, 84% residual activity after 1 h, highly stable also in presence of 3 M NaCl. The enzyme retains 65% activity after 24 h at 50°C, and its half-life is 5 h and 25 min at 55°C, and 12 min at 60°C | Haloterrigena turkmenica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Haloterrigena turkmenica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | over 50% of maximal activity within this range, inactive at pH 5.0, profile overview | Haloterrigena turkmenica |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
purified enzyme, 2 M NaCl, 55°C, 84% residual activity after 1 h | Haloterrigena turkmenica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the glycosyl hydrolase family 13, GH13. The enzyme has the characteristic structure of alpha-amylases belonging to the GH family 13 with a single polypeptide chain folded into the three domains A-C | Haloterrigena turkmenica |
| physiological function | alpha-amylases randomly cleave the internal glycosidic bond of the starch chain producing shorter oligosaccharides | Haloterrigena turkmenica |
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