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Literature summary for 3.2.1.54 extracted from
- Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity (2010), Appl. Microbiol. Biotechnol., 85, 1821-1830.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DMSO | 11% activation at 10% w/v | Thermofilum pendens |  |
| ethanol | 13% activation at 10% w/v | Thermofilum pendens | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Tpen_1458, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression as His-tagged enzyme in Escherichia coli strain MC1061 | Thermofilum pendens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | 23% inhibition at 5 mM | Thermofilum pendens | |
| Cu2+ | 83% inhibition at 5 mM | Thermofilum pendens | |
| Fe2+ | 81.6% inhibition at 5 mM | Thermofilum pendens | |
| Hg2+ | 82.5% inhibition at 5 mM | Thermofilum pendens | |
| Mn2+ | 50% inhibition at 5 mM | Thermofilum pendens | |
| Zn2+ | 82.2% inhibition at 5 mM | Thermofilum pendens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Al3+ | activates 46.8% at 5 mM | Thermofilum pendens | |
| Ca2+ | activates 36% at 5 mM | Thermofilum pendens | |
| Co2+ | 6% activation at 5 mM | Thermofilum pendens | |
| Mg2+ | activates 30% at 5 mM | Thermofilum pendens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermofilum pendens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme 3.0fold from Escherichia coli by heat treatment and nickel affinity chromatography | Thermofilum pendens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 177 | - |
95°C, pH 5.5, crude recombinant enzyme in Escherichia coli cell extract, substrate is gamma-cyclodextrin | Thermofilum pendens |
| 535.1 | - |
95°C, pH 5.5, purified recombinant enzyme, substrate is gamma-cyclodextrin | Thermofilum pendens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-cyclodextrin + H2O | 65% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose | - |
? | |
| alpha-cyclodextrin + H2O | 65% of the activity with gamma-cyclodextrin | Thermofilum pendens Hrk 5 (DSM 2475) | maltose + D-glucose | - |
? | |
| beta-cyclodextrin + H2O | 78% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose | - |
? | |
| beta-cyclodextrin + H2O | 78% of the activity with gamma-cyclodextrin | Thermofilum pendens Hrk 5 (DSM 2475) | maltose + D-glucose | - |
? | |
| gamma-cyclodextrin + H2O | during the initial stage of the reaction, only one alpha-1,4-glycosidic linkage of every gamma-cyclodexrtrin is cleaved, and then the linear maltooctaose is formed. Until almost all gamma-cyclodextrin has disappeared, maltooctaose is not further hydrolyzed. Selective degradation of gamma-cyclodextrin is preferred by the enzyme in the presence of maltooctaose. After all rings are opened at one single glycosidic linkage of cyclodextrins, the corresponding maltooligosaccharides started to be hydrolyzed into smaller maltooligosaccharides. The final hydrolysis products are maltose and glucose | Thermofilum pendens | maltose + D-glucose | - |
? | |
| maltoheptaose + H2O | 24% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose + ? | - |
? | |
| maltoheptaose + H2O | 24% of the activity with gamma-cyclodextrin | Thermofilum pendens Hrk 5 (DSM 2475) | maltose + D-glucose + ? | - |
? | |
| maltohexaose + H2O | 14% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose + ? | - |
? | |
| maltopentaose + H2O | 11% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose + ? | - |
? | |
| maltotetraose + H2O | 6% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + 2 D-glucose | - |
? | |
| maltotetraose + H2O | 6% of the activity with gamma-cyclodextrin | Thermofilum pendens Hrk 5 (DSM 2475) | maltose + 2 D-glucose | - |
? | |
| maltotriose + H2O | 5.3% of the activity with gamma-cyclodextrin | Thermofilum pendens | maltose + D-glucose | - |
? | |
| maltotriose + H2O | 5.3% of the activity with gamma-cyclodextrin | Thermofilum pendens Hrk 5 (DSM 2475) | maltose + D-glucose | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
- |
Thermofilum pendens |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | 105 | 80°C: about 50% of maximal activity, 105°C: about 50% of maximal activity | Thermofilum pendens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
160 min, about 50% loss of activity | Thermofilum pendens |
| 90 | - |
160 min, about 45% loss of activity | Thermofilum pendens |
| 95 | - |
80 min, about 55% loss of activity | Thermofilum pendens |
| 100 | - |
30 min, about 60% loss of activity | Thermofilum pendens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
substrate: gamma-cyclodextrin | Thermofilum pendens |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6.5 | pH 5.0: about 80% of maximal activity, pH 6.5: about 50% of maximal activity | Thermofilum pendens |
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