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Literature summary extracted from
- A thermoactive glucoamylase with biotechnological relevance from the thermoacidophilic euryarchaeon Thermoplasma acidophilum (2008), Appl. Microbiol. Biotechnol., 78, 105-114.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | 2-mercaptoethanol | - |
Thermoplasma acidophilum |  |
| 3.2.1.3 | DTT | - |
Thermoplasma acidophilum | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | gene taGA, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli | Thermoplasma acidophilum |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.2.1.3 | Ca2+ and Na+ highly increase the stability of the enzyme | Thermoplasma acidophilum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Ag+ | complete inhibition at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Cr3+ | complete inhibition at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Cu2+ | complete inhibition at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | EDTA | strong inhibition | Thermoplasma acidophilum | |
| 3.2.1.3 | N-bromosuccinimide | almost complete inhibition at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | NaN3 | strong inhibition | Thermoplasma acidophilum | |
| 3.2.1.3 | phenylmethyl sulfonyl fluoride | 53% inhibition at 5 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | SDS | complete inhibition at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Triton-X100 | inhibits enzyme activity for 25% and 26% at concentrations of 1 mM and 2.5 mM, respectively, complete inhibition at 5 mM | Thermoplasma acidophilum | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.3 | additional information | - |
additional information | - |
Thermoplasma acidophilum |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | additional information | no potential signal peptide sequence | Thermoplasma acidophilum | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Ca2+ | highly increases the stability of the enzyme | Thermoplasma acidophilum | |
| 3.2.1.3 | Co2+ | activates at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Fe3+ | activates at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Mn2+ | activates 3fold at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | additional information | no effects by guanidine chloride, Ca2+, Na+, and Mg2+ at 1 mM | Thermoplasma acidophilum | |
| 3.2.1.3 | Na+ | highly increases the stability of the enzyme | Thermoplasma acidophilum | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 66000 | - |
2 * 66000, enzyme active state, SDS-PAGE | Thermoplasma acidophilum |
| 3.2.1.3 | 130000 | - |
about, recombinant enzyme, native PAGE | Thermoplasma acidophilum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Thermoplasma acidophilum | - |
strain DSM 1728, gene taGA | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | additional information | no potential signal peptide sequence | Thermoplasma acidophilum |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | recombinant enzyme 22fold from Escherichia coli to homogeneity using heat treatment, anion exchange chromatography, and gel filtration | Thermoplasma acidophilum |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.21 | - |
purified recombinant enzyme, substrate amylopectin | Thermoplasma acidophilum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | amylopectin + H2O | best substrate, from potatoes or corn | Thermoplasma acidophilum | ? | - |
? | |
| 3.2.1.3 | amylose + H2O | - |
Thermoplasma acidophilum | ? | - |
? | |
| 3.2.1.3 | glycogen + H2O | - |
Thermoplasma acidophilum | ? | - |
? | |
| 3.2.1.3 | maltohexaose + H2O | - |
Thermoplasma acidophilum | maltopentaose + D-glucose | - |
? | |
| 3.2.1.3 | maltopentaose + H2O | - |
Thermoplasma acidophilum | maltotetraose + beta-D-glucose | - |
? | |
| 3.2.1.3 | maltotetraose + H2O | - |
Thermoplasma acidophilum | maltotriose + beta-D-glucose | - |
? | |
| 3.2.1.3 | additional information | the enzyme is an exo-hydrolase that attacks the substrate from the non-reducing end, producing glucose with beta-anomeric configuration, substrate specificity with substrates from different sources in descending activity order: Paselli starch, soluble starch, corn-amylopectin, glycogen, and amylose, no activity with pullulan, alpha-cyclodextrin, beta-cyclodextrin, and gamma-cyclodextrin, TaGA is not able to catalyze the formation of oligosaccharides, e.g., by transglycosylation with glucose as substrate | Thermoplasma acidophilum | ? | - |
? | |
| 3.2.1.3 | starch + H2O | Paselli starch or soluble starch | Thermoplasma acidophilum | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | dimer | 2 * 66000, enzyme active state, SDS-PAGE | Thermoplasma acidophilum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | amyloglucosidase | - |
Thermoplasma acidophilum |
| 3.2.1.3 | gamma-amylase | - |
Thermoplasma acidophilum |
| 3.2.1.3 | glucoamylase | - |
Thermoplasma acidophilum |
| 3.2.1.3 | TagA | - |
Thermoplasma acidophilum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 75 | - |
purified recombinant enzyme | Thermoplasma acidophilum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 20 | 100 | activity range, purified recombinant enzyme | Thermoplasma acidophilum |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | additional information | - |
Ca2+ and Na+ highly increase the thermal stability of the enzyme | Thermoplasma acidophilum |
| 3.2.1.3 | 50 | - |
purified recombinant enzyme, 48 h, 25% increased activity | Thermoplasma acidophilum |
| 3.2.1.3 | 80 | - |
purified recombinant enzyme, half-life in absence of Ca2+ is 15 min, in presence of 5 mM Ca2+ is 2 h | Thermoplasma acidophilum |
| 3.2.1.3 | 90 | - |
purified recombinant enzyme, 4 min, 2% of maximal activity remaining in absence of Ca2+, 68% in presence of 5 mM Ca2+ | Thermoplasma acidophilum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4 | - |
purified recombinant enzyme, maximum 1 | Thermoplasma acidophilum |
| 3.2.1.3 | 6 | - |
purified recombinant enzyme, maximum 2 | Thermoplasma acidophilum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 3.5 | 8.3 | activity range, purified recombinant enzyme | Thermoplasma acidophilum |
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