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Literature summary for 5.4.99.16 extracted from
- Structural characteristics and function of a new kind of thermostable trehalose synthase from Thermobaculum terrenum (2017), J. Agric. Food Chem., 65, 7726-7735 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene treS, recombinant overexpression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Thermobaculum terrenum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H534Y | site-directed mutagenesis, the mutant enzyme retains 50% activity after 30 min at 70°C | Thermobaculum terrenum |
| R283G/Y287R/R291G | site-directed mutagenesis, the mutant enzyme retains 36% activity after 30 min at 70°C | Thermobaculum terrenum |
| R283G/Y287R/R291G/H534Y | site-directed mutagenesis, the mutant enzyme retains 25% activity after 30 min at 70°C | Thermobaculum terrenum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | 34% inhibition at 1 mM, 41% at 10 mM | Thermobaculum terrenum |  |
| EDTA | 46% inhibition at 1 mM, 100% at 10 mM | Thermobaculum terrenum | |
| Ni2+ | 66% inhibition at 1 mM, 75% at 10 mM | Thermobaculum terrenum | |
| SDS | 77% inhibition at 1 mM, 100% at 10 mM | Thermobaculum terrenum | |
| Tris | structural characteristics of enzyme TtTS in complex with the inhibitor TriS | Thermobaculum terrenum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 8% activating at 10 mM | Thermobaculum terrenum | |
| Fe2+ | 9% activating at 10 mM | Thermobaculum terrenum | |
| Mg2+ | 8% activating at 10 mM | Thermobaculum terrenum | |
| Mn2+ | 8% activating at 10 mM | Thermobaculum terrenum | |
| additional information | no effects by Ba2+ and K+ at up to 10 mM | Thermobaculum terrenum | |
| additional information | the enzyme has four potential metal ion-binding sites | Thermobaculum terrenum | |
| Zn2+ | 19% activating at 10 mM | Thermobaculum terrenum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltose | Thermobaculum terrenum | - |
alpha,alpha-trehalose | - |
r | |
| maltose | Thermobaculum terrenum ATCC BAA-798 / YNP1 | - |
alpha,alpha-trehalose | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermobaculum terrenum | D1CE96 | - |
- |
| Thermobaculum terrenum ATCC BAA-798 / YNP1 | D1CE96 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration | Thermobaculum terrenum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltose | - |
Thermobaculum terrenum | alpha,alpha-trehalose | - |
r | |
| maltose | - |
Thermobaculum terrenum ATCC BAA-798 / YNP1 | alpha,alpha-trehalose | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme TtTS exhibits the typical three domain glycoside hydrolase family 13 structure, three-dimensional structure analysis, structure comparisons, overview | Thermobaculum terrenum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trehalose synthase | - |
Thermobaculum terrenum |
| TreS | - |
Thermobaculum terrenum |
| TtTS | - |
Thermobaculum terrenum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
recombinant enzyme | Thermobaculum terrenum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 80 | 95% activity at 30°C, maximal activity at 45°C, 80% at 65°C, 30% activity at 70°C, inactivation at 85°C | Thermobaculum terrenum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 75 | purified recombinant His6-tagged enzyme, over 80% activity remaining after 8 h at 40-70°C, 40% activity remaining at 75°C, inactivation at 80°C | Thermobaculum terrenum |
| 70 | - |
enzyme mutants R283G/Y287R/R291G, H534Y, and R283G/Y287R/R291G/H534Y retain 36%, 50%, and 25% activity, respectively, at 70°C after 30 min | Thermobaculum terrenum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
recombinant enzyme | Thermobaculum terrenum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 9.5 | over 70% of maximal activity at pH 5.5-9.0, 50% of maximal activity at pH 5.0 and pH 9.5 | Thermobaculum terrenum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme TtTS belongs to the glycoside hydrolase family 13 and exhibits the typical three domain structure | Thermobaculum terrenum |
| additional information | the enzyme's catalytic cleft consists of Asp202-Glu244-Asp310 and various conserved substrate-binding residues, three-dimensional structure enzyme structure and active site structure | Thermobaculum terrenum |
| physiological function | the thermostable enzyme trehalose synthase from Thermobaculum terrenum (TtTS) catalyzes the reversible interconversion of maltose and trehalose | Thermobaculum terrenum |
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