Activating Compound | Comment | Organism | Structure |
---|---|---|---|
glycosyltransferase | the Thermoproteus tenax trehalose-6-phosphate synthase/phosphatase (TPSP) exhibits high phosphatase activity, but requires activation by the co-expressed glycosyltransferase for bifunctional synthase/phosphatase activity. The glycosyltransferase mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the TPSP enzyme. Activation is mediated by complex-formation in vivo | Thermoproteus tenax |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermoproteus tenax |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
33000 | - |
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain | Thermoproteus tenax |
50000 | - |
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain | Thermoproteus tenax |
81000 | - |
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain | Thermoproteus tenax |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoproteus tenax | G4RK44 | - |
- |
Thermoproteus tenax | G4RK44 | bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12 | - |
Thermoproteus tenax ATCC 35583 | G4RK44 | bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12 | - |
Thermoproteus tenax DSM 2078 | G4RK44 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
3.5 | - |
pH 7.0, 80°C | Thermoproteus tenax |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha,alpha-trehalose 6-phosphate + H2O | - |
Thermoproteus tenax | alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | - |
Thermoproteus tenax DSM 2078 | alpha,alpha-trehalose + phosphate | - |
? | |
alpha,alpha-trehalose 6-phosphate + H2O | - |
Thermoproteus tenax ATCC 35583 | alpha,alpha-trehalose + phosphate | - |
? | |
UDP-alpha-D-glucose + D-fructose 6-phosphate | - |
Thermoproteus tenax | UDP + alpha,alpha-1,1-trehalose 6-phosphate | presence of glycosyltransferase protein is required | ? | |
UDP-alpha-D-glucose + D-fructose 6-phosphate | - |
Thermoproteus tenax DSM 2078 | UDP + alpha,alpha-1,1-trehalose 6-phosphate | presence of glycosyltransferase protein is required | ? | |
UDP-alpha-D-glucose + D-fructose 6-phosphate | - |
Thermoproteus tenax ATCC 35583 | UDP + alpha,alpha-1,1-trehalose 6-phosphate | presence of glycosyltransferase protein is required | ? |
Subunits | Comment | Organism |
---|---|---|
? | x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain | Thermoproteus tenax |
Synonyms | Comment | Organism |
---|---|---|
TPSP | - |
Thermoproteus tenax |
TPSP | the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain | Thermoproteus tenax |
trehalose-6-phosphate synthase/phosphatase | the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain | Thermoproteus tenax |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
assay at | Thermoproteus tenax |
General Information | Comment | Organism |
---|---|---|
physiological function | the fused trehalose-6-phosphate synthase/phosphatase TPSP consists of an N-terminal trehalose-6-phosphate synthase (TPS) and a C-terminal trehalose-6-phosphate phosphatase (TPP) domain. The gene is organized in an operon with a putative glycosyltransferase GT and a putative mechanosensitive channel MSC. The enzyme exhibits high phosphatase activity, but requires activation by the co-expressed GT for bifunctional synthase-phosphatase activity. The GT mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the enzyme. Activation is mediated by complex-formation | Thermoproteus tenax |