Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5-fluoro-alpha-D-glucosyl fluoride | behaves like a reversible inhibitor | Mycolicibacterium smegmatis | |
casuarine | - |
Mycolicibacterium smegmatis | |
D-gluconohydroximino-1,5-lactam | - |
Mycolicibacterium smegmatis | |
deoxynojirimycin | - |
Mycolicibacterium smegmatis | |
isofagomine | - |
Mycolicibacterium smegmatis | |
xylodeoxynojirimycin | - |
Mycolicibacterium smegmatis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state kinetics with 5-fluoroglycosyl fluorides, alpha-aryl glucosides, and alpha-glucosyl fluoride | Mycolicibacterium smegmatis | |
0.008 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
0.087 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
65237 | - |
x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
68202 | - |
x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | Mycolicibacterium smegmatis | - |
alpha,alpha-trehalose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycolicibacterium smegmatis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
maltose = alpha,alpha-trehalose | two-step, double displacement catalytic mechanism, overview | Mycolicibacterium smegmatis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | - |
Mycolicibacterium smegmatis | alpha,alpha-trehalose | - |
r | |
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 | Comment | Organism |
---|---|---|
? | x * 68202, sequence calculation, x * 65237, mass spectrometry | Mycolicibacterium smegmatis |
Synonyms | Comment | Organism |
---|---|---|
Trehalose synthase | - |
Mycolicibacterium smegmatis |
TreS | - |
Mycolicibacterium smegmatis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mycolicibacterium smegmatis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
19 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
66 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Mycolicibacterium smegmatis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00025 | - |
deoxynojirimycin | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
0.0021 | - |
D-gluconohydroximino-1,5-lactam | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
0.0025 | - |
casuarine | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
0.14 | - |
isofagomine | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
0.3 | - |
xylodeoxynojirimycin | pH 6.8, 37°C | Mycolicibacterium smegmatis |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a retaining alpha-transglycosidase in the alpha-amylase family (GH13) | Mycolicibacterium smegmatis |
physiological function | the enzyme functions primarily in the mobilization of trehalose as a glycogen precursor | Mycolicibacterium smegmatis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.75 | - |
alpha,alpha-trehalose | pH 6.8, 37°C | Mycolicibacterium smegmatis | |
2.4 | - |
maltose | pH 6.8, 37°C | Mycolicibacterium smegmatis |