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Literature summary extracted from

  • Zaparty, M.; Hagemann, A.; Bräsen, C.; Hensel, R.; Lupas, A.N.; Brinkmann, H.; Siebers, B.
    The first prokaryotic trehalose synthase complex identified in the hyperthermophilic crenarchaeon Thermoproteus tenax. (2013), PLoS One, 8, e61354.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.15 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(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.15 expression in Escherichia coli Thermoproteus tenax
3.1.3.12 expression in Escherichia coli Thermoproteus tenax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.15 33000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
2.4.1.15 50000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
2.4.1.15 81000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
3.1.3.12 33000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
3.1.3.12 50000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
3.1.3.12 81000
-
 x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.15 Thermoproteus tenax G4RK44
-
-
2.4.1.15 Thermoproteus tenax G4RK44 bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
-
2.4.1.15 Thermoproteus tenax ATCC 35583 G4RK44 bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
-
2.4.1.15 Thermoproteus tenax DSM 2078 G4RK44
-
-
3.1.3.12 Thermoproteus tenax G4RK44
-
-
3.1.3.12 Thermoproteus tenax G4RK44 bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
-
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
-
3.1.3.12 Thermoproteus tenax DSM 2078 G4RK44
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.15 3.5
-
 pH 7.0, 80°C Thermoproteus tenax
3.1.3.12 2.9
-
 pH 7.0, 80°C Thermoproteus tenax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.15 alpha,alpha-trehalose 6-phosphate + H2O
-
 Thermoproteus tenax alpha,alpha-trehalose + phosphate
-
 ?
2.4.1.15 alpha,alpha-trehalose 6-phosphate + H2O
-
 Thermoproteus tenax DSM 2078 alpha,alpha-trehalose + phosphate
-
 ?
2.4.1.15 alpha,alpha-trehalose 6-phosphate + H2O
-
 Thermoproteus tenax ATCC 35583 alpha,alpha-trehalose + phosphate
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-fructose 6-phosphate
-
 Thermoproteus tenax UDP + alpha,alpha-1,1-trehalose 6-phosphate presence of glycosyltransferase protein is required ?
2.4.1.15 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 ?
2.4.1.15 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 ?
3.1.3.12 alpha,alpha-1,1-trehalose 6-phosphate
-
 Thermoproteus tenax alpha,alpha-1,1-trehalose + phosphate
-
 ?
3.1.3.12 alpha,alpha-1,1-trehalose 6-phosphate
-
 Thermoproteus tenax DSM 2078 alpha,alpha-1,1-trehalose + phosphate
-
 ?
3.1.3.12 alpha,alpha-1,1-trehalose 6-phosphate
-
 Thermoproteus tenax ATCC 35583 alpha,alpha-1,1-trehalose + phosphate
-
 ?
3.1.3.12 additional information enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15 Thermoproteus tenax ?
-
 ?
3.1.3.12 additional information enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15 Thermoproteus tenax DSM 2078 ?
-
 ?
3.1.3.12 additional information enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15 Thermoproteus tenax ATCC 35583 ?
-
 ?
3.1.3.12 UDP-alpha-D-glucose + D-glucose 6-phosphate
-
 Thermoproteus tenax UDP + alpha,alpha-trehalose 6-phosphate
-
 ?
3.1.3.12 UDP-alpha-D-glucose + D-glucose 6-phosphate
-
 Thermoproteus tenax DSM 2078 UDP + alpha,alpha-trehalose 6-phosphate
-
 ?
3.1.3.12 UDP-alpha-D-glucose + D-glucose 6-phosphate
-
 Thermoproteus tenax ATCC 35583 UDP + alpha,alpha-trehalose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.15 ? x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax
3.1.3.12 ? x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain Thermoproteus tenax

Synonyms

EC Number Synonyms Comment Organism
2.4.1.15 TPSP
-
 Thermoproteus tenax
2.4.1.15 TPSP the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain Thermoproteus tenax
2.4.1.15 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
3.1.3.12 TPSP
-
 Thermoproteus tenax
3.1.3.12 TPSP the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain Thermoproteus tenax
3.1.3.12 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.15 80
-
 assay at Thermoproteus tenax
3.1.3.12 80
-
 assay at Thermoproteus tenax

General Information

EC Number General Information Comment Organism
2.4.1.15 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
3.1.3.12 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