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Literature summary extracted from
- Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis (2011), J. Biol. Chem., 286, 35601-35609.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.99.16 | 5-fluoro-alpha-D-glucosyl fluoride | behaves like a reversible inhibitor | Mycolicibacterium smegmatis |  |
| 5.4.99.16 | casuarine | - |
Mycolicibacterium smegmatis | |
| 5.4.99.16 | D-gluconohydroximino-1,5-lactam | - |
Mycolicibacterium smegmatis | |
| 5.4.99.16 | deoxynojirimycin | - |
Mycolicibacterium smegmatis | |
| 5.4.99.16 | isofagomine | - |
Mycolicibacterium smegmatis | |
| 5.4.99.16 | xylodeoxynojirimycin | - |
Mycolicibacterium smegmatis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | additional information | - |
additional information | Michaelis-Menten steady-state kinetics with 5-fluoroglycosyl fluorides, alpha-aryl glucosides, and alpha-glucosyl fluoride | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.008 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.087 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 65237 | - |
x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
| 5.4.99.16 | 68202 | - |
x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | Mycolicibacterium smegmatis | - |
alpha,alpha-trehalose | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.4.99.16 | Mycolicibacterium smegmatis | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.4.99.16 | maltose = alpha,alpha-trehalose | two-step, double displacement catalytic mechanism, overview | Mycolicibacterium smegmatis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | - |
Mycolicibacterium smegmatis | alpha,alpha-trehalose | - |
r | |
| 5.4.99.16 | additional information | the enzyme catalyzes the hydrolytic cleavage of alpha-aryl glucosides as well as alpha-glucosyl fluoride, overview. Reaction of TreS with 5-fluoro-alpha-D-glucosyl fluoride results in the trapping of a covalent glycosyl-enzyme intermediate consistent with TreS being a member of the retaining glycoside hydrolase family 13 enzyme family, thus likely following a two-step, double displacement mechanism. Inability of TreS to incorporate isotope-labeled exogenous glucose into maltose or trehalose, the absence of a secondary deuterium kinetic isotope effect and the general independence of kcat upon leaving group ability both point to a rate-determining conformational change, likely the opening and closing of the enzyme active site | Mycolicibacterium smegmatis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | ? | x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | Trehalose synthase | - |
Mycolicibacterium smegmatis |
| 5.4.99.16 | TreS | - |
Mycolicibacterium smegmatis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 37 | - |
assay at | Mycolicibacterium smegmatis |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 19 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 66 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 6.8 | - |
assay at | Mycolicibacterium smegmatis |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 5.4.99.16 | 0.00025 | - |
deoxynojirimycin | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.0021 | - |
D-gluconohydroximino-1,5-lactam | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.0025 | - |
casuarine | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.14 | - |
isofagomine | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 0.3 | - |
xylodeoxynojirimycin | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | evolution | the enzyme is a retaining alpha-transglycosidase in the alpha-amylase family (GH13) | Mycolicibacterium smegmatis |
| 5.4.99.16 | physiological function | the enzyme functions primarily in the mobilization of trehalose as a glycogen precursor | Mycolicibacterium smegmatis |
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 | 0.75 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
| 5.4.99.16 | 2.4 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
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