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Literature summary for 3.1.3.12 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
Search for more literature for 3.1.3.12

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermoproteus tenax

Molecular Weight [Da]

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

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 [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 assay at Thermoproteus tenax

General Information

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