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Literature summary for 5.4.99.16 extracted from
- Gene cloning and characterization of a trehalose synthase from Corynebacterium glutamicum ATCC13032 (2010), Food Sci. Biotechnol., 19, 565-569.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli MC1061 cells | Corynebacterium glutamicum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 93% residual activity at 5 mM | Corynebacterium glutamicum |  |
| Cu2+ | 45.4% residual activity at 5 mM | Corynebacterium glutamicum | |
| EDTA | 68.5% residual activity at 5 mM | Corynebacterium glutamicum | |
| Mn2+ | 60.9% residual activity at 5 mM | Corynebacterium glutamicum | |
| Ni2+ | 49.4% residual activity at 5 mM | Corynebacterium glutamicum | |
| SDS | 0.25% residual activity at 5 mM | Corynebacterium glutamicum | |
| Zn2+ | 71.6% residual activity at 5 mM | Corynebacterium glutamicum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | 114% activity at 1 mM | Corynebacterium glutamicum | |
| Mg2+ | 112% activity at 1 mM | Corynebacterium glutamicum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
x * 70000, calculated from amino acid sequence | Corynebacterium glutamicum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | - |
- |
- |
| Corynebacterium glutamicum ATCC 13032 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA column chromatography | Corynebacterium glutamicum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltose | the maximum conversion yield reaches 69% at 25°C after 9 h of reaction | Corynebacterium glutamicum | alpha,alpha-trehalose | - |
r | |
| maltose | the maximum conversion yield reaches 69% at 25°C after 9 h of reaction | Corynebacterium glutamicum ATCC 13032 | alpha,alpha-trehalose | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 70000, calculated from amino acid sequence | Corynebacterium glutamicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trehalose synthase | - |
Corynebacterium glutamicum |
| TreS | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
- |
Corynebacterium glutamicum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
about 80% of activity is retained at 40°C, but the enzyme is not stable at higher temperature than 40°C | Corynebacterium glutamicum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
at 35°C in Na-phosphate buffer | Corynebacterium glutamicum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 9 | more than 80% of activity is maintained from pH 6.5 and 7.5, the activities of the enzyme markedly decrease in 50 mM Tris-HCl buffer from pH 7.0-9.0 | Corynebacterium glutamicum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8.5 | - |
Corynebacterium glutamicum |
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