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Literature summary extracted from
- Improving trehalose synthase activity by adding the C-terminal domain of trehalose synthase from Thermus thermophilus (2017), Biores. Technol., 245, 1749-1756 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | gene treS, recombinant expression of His-tagged enzyme fusion mutant linked to the domain C from the enzyme of Thermus thermophilus in Escherichia coli strain Rosetta (DE3) | Streptomyces coelicolor |
| 5.4.99.16 | gene treS, recombinant expression of His-tagged enzyme fusion mutant linked to the domain C from the enzyme of Thermus thermophilus in Escherichia coli strain Rosetta (DE3) | Thermotoga maritima |
| 5.4.99.16 | gene treS, recombinant expression of His-tagged enzyme fusion mutant linked to the domain C from the enzyme of Thermus thermophilus in Escherichia coli strain Rosetta (DE3) | Corynebacterium glutamicum |
| 5.4.99.16 | gene treS, recombinant expression of His-tagged enzyme fusion mutant linked to the domain C from the enzyme of Thermus thermophilus in Escherichia coli strain Rosetta (DE3) | Pseudomonas putida |
| 5.4.99.16 | gene treS, sequence comparisons, recombinant expression of His-tagged wild-type enzyme and mutant enzymes from other species that are fused to the domain C from the Thermus thermophilus enzyme, in Escherichia coli strain Rosetta (DE3) | Thermus thermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | additional information | addition of the C-terminal domain of Thermus thermophilus TtTreS to the Corynebacterium glutamicum enzyme CgTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for CgTreS activity enhancement. The specific activity is slightly improved by linking to the TtTreS-C fragment | Corynebacterium glutamicum |
| 5.4.99.16 | additional information | addition of the C-terminal domain of Thermus thermophilus TtTreS to the Pseudomonas putida enzyme PpTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment | Pseudomonas putida |
| 5.4.99.16 | additional information | addition of the C-terminal domain of Thermus thermophilus TtTreS to the Streptomyces coelicolor enzyme ScTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved about twofold by linking to the TtTreS-C fragment | Streptomyces coelicolor |
| 5.4.99.16 | additional information | addition of the C-terminal domain of Thermus thermophilus TtTreS to the Thermotoga maritima enzyme TmTreS. A flexible linker peptide between the TreS enzyme and TtTreS-C domain is essential for PpTreS activity enhancement. The specific activity is improved by linking to the TtTreS-C fragment | Thermotoga maritima |
| 5.4.99.16 | additional information | addition of the C-terminal domain of TtTreS to the Deinococcus radiodurans enzyme DrTreS leads to great improvement of the thermostability of the cold-active DrTreS | Deinococcus radiodurans |
| 5.4.99.16 | additional information | the C-domain of enzyme TtTreS, TtTreS-C, is fused to four different enzymes from other species, i.e. PpTreS, CgTreS, ScTreS, and TmTreS from Pseudomonas putida NBRC 14164, Corynebacterium glutamicum ATCC 13032, Streptomyces coelicolor ATCC 23899, and Thermotoga maritima MSB8, domain structures, overview. A flexible linker peptide between the TreS enzyme and TtTreS-C is essential for its activity enhancement. The specific activities of the four enzymes are improved by linking to the TtTreS-C fragment. When added with the C-terminal domain of TtTreS, the thermostability of a cold-active TreS from Deinococcus radiodurans (DrTreS) is greatly improved | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | Streptomyces coelicolor | - |
alpha,alpha-trehalose | - |
r |  |
| 5.4.99.16 | maltose | Thermotoga maritima | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Corynebacterium glutamicum | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus radiodurans | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Thermus thermophilus | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Pseudomonas putida | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Corynebacterium glutamicum ATCC 13032 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Streptomyces coelicolor ATCC 23899 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Pseudomonas putida NBRC 14164 | - |
alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | - |
alpha,alpha-trehalose | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.16 | Corynebacterium glutamicum | A0A1R4FYB1 | - |
- |
| 5.4.99.16 | Corynebacterium glutamicum ATCC 13032 | A0A1R4FYB1 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans | I3NX86 | - |
- |
| 5.4.99.16 | Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | I3NX86 | - |
- |
| 5.4.99.16 | Pseudomonas putida | A0A2Z4RCL2 | - |
- |
| 5.4.99.16 | Pseudomonas putida NBRC 14164 | A0A2Z4RCL2 | - |
- |
| 5.4.99.16 | Streptomyces coelicolor | - |
- |
- |
| 5.4.99.16 | Streptomyces coelicolor ATCC 23899 | - |
- |
- |
| 5.4.99.16 | Thermotoga maritima | - |
- |
- |
| 5.4.99.16 | Thermus thermophilus | O06458 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | recombinant His-tagged domainC-fusion mutant enzyme CgTreS-TtTreS-C from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Corynebacterium glutamicum |
| 5.4.99.16 | recombinant His-tagged domainC-fusion mutant enzyme PpTreS-TtTreS-C from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Pseudomonas putida |
| 5.4.99.16 | recombinant His-tagged domainC-fusion mutant enzyme ScTreS-TtTreS-C from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Streptomyces coelicolor |
| 5.4.99.16 | recombinant His-tagged domainC-fusion mutant enzyme TmTreS-TtTreS-C from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Thermotoga maritima |
| 5.4.99.16 | recombinant His-tagged wild-type enzyme and domainC-fusion mutant enzymes from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration | Thermus thermophilus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | - |
Streptomyces coelicolor | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermotoga maritima | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Corynebacterium glutamicum | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus radiodurans | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Thermus thermophilus | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Pseudomonas putida | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Corynebacterium glutamicum ATCC 13032 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Streptomyces coelicolor ATCC 23899 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Pseudomonas putida NBRC 14164 | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | maltose | - |
Deinococcus radiodurans ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422 | alpha,alpha-trehalose | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | More | the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | DKY63_02445 | - |
Pseudomonas putida |
| 5.4.99.16 | DrTreS | - |
Streptomyces coelicolor |
| 5.4.99.16 | DrTreS | - |
Thermotoga maritima |
| 5.4.99.16 | DrTreS | - |
Corynebacterium glutamicum |
| 5.4.99.16 | DrTreS | - |
Deinococcus radiodurans |
| 5.4.99.16 | DrTreS | - |
Pseudomonas putida |
| 5.4.99.16 | Trehalose synthase | - |
Streptomyces coelicolor |
| 5.4.99.16 | Trehalose synthase | - |
Thermotoga maritima |
| 5.4.99.16 | Trehalose synthase | - |
Corynebacterium glutamicum |
| 5.4.99.16 | Trehalose synthase | - |
Deinococcus radiodurans |
| 5.4.99.16 | Trehalose synthase | - |
Thermus thermophilus |
| 5.4.99.16 | Trehalose synthase | - |
Pseudomonas putida |
| 5.4.99.16 | TreS | - |
Streptomyces coelicolor |
| 5.4.99.16 | TreS | - |
Thermotoga maritima |
| 5.4.99.16 | TreS | - |
Thermus thermophilus |
| 5.4.99.16 | TreS | - |
Pseudomonas putida |
| 5.4.99.16 | TtTreS | - |
Thermus thermophilus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 20 | - |
assay at | Thermus thermophilus |
| 5.4.99.16 | 20 | - |
wild-type enzyme and recombinant fusion enzyme mutant | Streptomyces coelicolor |
| 5.4.99.16 | 20 | - |
wild-type enzyme and recombinant fusion enzyme mutant | Corynebacterium glutamicum |
| 5.4.99.16 | 20 | - |
wild-type enzyme and recombinant fusion enzyme mutant | Pseudomonas putida |
| 5.4.99.16 | 30 | - |
recombinant fusion enzyme mutant | Thermotoga maritima |
| 5.4.99.16 | 40 | - |
wild-type enzyme | Thermotoga maritima |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 20 | 50 | wild-type: high activity at 20-30°C, very low activity at 40-50°C. Fusion mutant: high activity at 20-40°C, moderate activity at 50°C | Corynebacterium glutamicum |
| 5.4.99.16 | 20 | 50 | wild-type: moderate activity at 20-30°C and 50°C, high activity at 40°C. Fusion mutant: high activity at 20-30°C, moderate activity at 40-50°C | Thermotoga maritima |
| 5.4.99.16 | 20 | 50 | wild-type: moderate activity at 20-30°C, moderate to low activity at 40-50°C. Fusion mutant: high activity at 20-30°C, moderate activity at 40-50°C | Streptomyces coelicolor |
| 5.4.99.16 | 20 | 50 | wild-type: moderate activity at 20-30°C, very low activity at 40-50°C. Fusion mutant: high activity at 20-40°C, low activity at 50°C | Pseudomonas putida |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | additional information | - |
the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS | Thermus thermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 7.4 | - |
assay at | Streptomyces coelicolor |
| 5.4.99.16 | 7.4 | - |
assay at | Thermotoga maritima |
| 5.4.99.16 | 7.4 | - |
assay at | Corynebacterium glutamicum |
| 5.4.99.16 | 7.4 | - |
assay at | Thermus thermophilus |
| 5.4.99.16 | 7.4 | - |
assay at | Pseudomonas putida |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | additional information | the enzyme TtTreS contains a unique C-terminal domain apart from the active domain, it plays a key role in maintaining the thermophilicity and thermostability of TtTreS | Thermus thermophilus |
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