Any feedback?
Literature summary extracted from
- Overexpression and characterization of a thermostable trehalose synthase from Meiothermus ruber (2010), Extremophiles, 14, 1-8.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | expressed in Escherichia coli Rosetta gami (DE3) cells | Meiothermus ruber |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.16 | Al3+ | complete inhibition at 2 mM | Meiothermus ruber |  |
| 5.4.99.16 | Ca2+ | about 10% residual activity at 10 mM | Meiothermus ruber | |
| 5.4.99.16 | Co2+ | about 5% residual activity at 10 mM | Meiothermus ruber | |
| 5.4.99.16 | Cu2+ | complete inhibition at 2 mM | Meiothermus ruber | |
| 5.4.99.16 | D-glucose | in the presence of 10 mM D-glucose, TreS shows a 3.6fold increase in Km and a nearly unchanged Vmax for maltose, implying that D-glucose is a competitive inhibitor of TreS | Meiothermus ruber | |
| 5.4.99.16 | Fe2+ | complete inhibition at 2 mM | Meiothermus ruber | |
| 5.4.99.16 | Mn2+ | about 10% residual activity at 10 mM | Meiothermus ruber | |
| 5.4.99.16 | Ni2+ | about 10% residual activity at 10 mM | Meiothermus ruber | |
| 5.4.99.16 | Zn2+ | complete inhibition at 2 mM | Meiothermus ruber | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 98.9 | - |
alpha,alpha-trehalose | - |
Meiothermus ruber | |
| 5.4.99.16 | 126.2 | - |
maltose | - |
Meiothermus ruber | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 110000 | - |
SDS-PAGE | Meiothermus ruber |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.16 | Meiothermus ruber | B1PK99 | - |
- |
| 5.4.99.16 | Meiothermus ruber CBS-01 | B1PK99 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.4.99.16 | Ni-NTA column chromatography | Meiothermus ruber |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate | Meiothermus ruber | alpha,alpha-trehalose | TreS also has a weak hydrolytic property with D-glucose as the byproduct | r | |
| 5.4.99.16 | maltose | the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate | Meiothermus ruber CBS-01 | alpha,alpha-trehalose | TreS also has a weak hydrolytic property with D-glucose as the byproduct | r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | Trehalose synthase | - |
Meiothermus ruber |
| 5.4.99.16 | TreS | - |
Meiothermus ruber |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 50 | - |
- |
Meiothermus ruber |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 60 | - |
the enzyme maintains very high activity (above 90%) at 60°C for 5 h | Meiothermus ruber |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 68.9 | - |
alpha,alpha-trehalose | - |
Meiothermus ruber | |
| 5.4.99.16 | 147 | - |
maltose | - |
Meiothermus ruber | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 6.5 | - |
- |
Meiothermus ruber |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 6 | 7 | - |
Meiothermus ruber |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 4 | 8 | the enzyme can maintain very high activity (above 90%) at pH 4.0-8.0 for 5 h, below pH 5.0 the enzyme shows no activity | Meiothermus ruber |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 3.76 | - |
D-glucose | - |
Meiothermus ruber | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 0.7 | - |
alpha,alpha-trehalose | - |
Meiothermus ruber | |
| 5.4.99.16 | 1.17 | - |
maltose | - |
Meiothermus ruber | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
