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Literature summary extracted from

  • Gao, Y.; Jiang, Y.; Liu, Q.; Wang, R.; Liu, X.; Liu, B.
    Enzymatic and regulatory properties of the trehalose-6-phosphate synthase from the thermoacidophilic archaeon Thermoplasma acidophilum (2014), Biochimie, 101, 215-220.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.15 chondroitin sulfate maximal activation at 0.0005 mg Thermoplasma acidophilum
2.4.1.15 chondroitin sulfate maximal stimulation at 400 ng Thermoplasma acidophilum
2.4.1.15 heparin 0.006 mg, stimulates Thermoplasma acidophilum
2.4.1.15 heparin heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng Thermoplasma acidophilum
2.4.1.15 additional information the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate Thermoplasma acidophilum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.15
-
 Thermoplasma acidophilum
2.4.1.15 gene TA1210, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strains DH5alpha and BL21-CodonPlus (DE3)-RIL Thermoplasma acidophilum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.15 2-mercaptoethanol 10% (v/v), 9% inhibition; 91% inhibition Thermoplasma acidophilum
2.4.1.15 Ba2+ 10 mM, 38% inhibition; 38% inhibition at 10 mM Thermoplasma acidophilum
2.4.1.15 dithiothreitol 10 mM, 27% inhibition Thermoplasma acidophilum
2.4.1.15 DTT 73% inhibition Thermoplasma acidophilum
2.4.1.15 EDTA 10 mM, 15% inhibition; 85% inhibition Thermoplasma acidophilum
2.4.1.15 ethanol 10% (v/v), 28% inhibition; 72% inhibition Thermoplasma acidophilum
2.4.1.15 guanidine hydrochloride 10 mM, 63% inhibition; 37% inhibition Thermoplasma acidophilum
2.4.1.15 Isopropanol 10% (v/v), 14% inhibition; 86% inhibition Thermoplasma acidophilum
2.4.1.15 K+ 10% inhibition at 10 mM; 10 mM, 10% inhibition Thermoplasma acidophilum
2.4.1.15 methanol 10% (v/v), 30% inhibition; 70% inhibition Thermoplasma acidophilum
2.4.1.15 n-butanol 10% (v/v), 48% inhibition; 52% inhibition Thermoplasma acidophilum
2.4.1.15 Na+ 10 mM, 8% inhibition; 8% inhibition at 10 mM Thermoplasma acidophilum
2.4.1.15 Ni2+ 10 mM, 21% inhibition; 21% inhibition at 10 mM Thermoplasma acidophilum
2.4.1.15 SDS 10% (w/v), 27% inhibition; 73% inhibition Thermoplasma acidophilum
2.4.1.15 Urea 10 mM, 15% inhibition; 85% inhibition Thermoplasma acidophilum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.15 0.2 1 UDP-alpha-D-glucose pH 6.0, 60°C, wild-type enzyme Thermoplasma acidophilum
2.4.1.15 0.27
-
 D-glucose 6-phosphate pH 6.0, 60°C, wild-type enzyme Thermoplasma acidophilum
2.4.1.15 0.34
-
 D-glucose 6-phosphate pH 6.0, 60°C, N-loop truncation mutant enzyme Thermoplasma acidophilum
2.4.1.15 0.74
-
 UDP-alpha-D-glucose pH 6.0, 60°C, N-loop truncation mutant enzyme Thermoplasma acidophilum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.15 Co2+ the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+ Thermoplasma acidophilum
2.4.1.15 Co2+ 1.91fold activation at 10 mM Thermoplasma acidophilum
2.4.1.15 Mg2+ the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+ Thermoplasma acidophilum
2.4.1.15 Mg2+ 2.33fold activation at 10 mM Thermoplasma acidophilum
2.4.1.15 Mn2+ the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+ Thermoplasma acidophilum
2.4.1.15 Mn2+ 1.16fold activation at 10 mM Thermoplasma acidophilum
2.4.1.15 additional information the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity Thermoplasma acidophilum
2.4.1.15 additional information no effect by Li+ at 10 mM Thermoplasma acidophilum
2.4.1.15 Zn2+ the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+ Thermoplasma acidophilum
2.4.1.15 Zn2+ 2.26fold activation at 10 mM Thermoplasma acidophilum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.15 51400
-
 2 * 51400, about, sequence calculation Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.15 UDP-glucose + D-glucose 6-phosphate Thermoplasma acidophilum
-
 UDP + alpha,alpha-trehalose 6-phosphate
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
2.4.1.15 Ethanol 72% inhibition Thermoplasma acidophilum
2.4.1.15 isopropanol 86% inhibition Thermoplasma acidophilum
2.4.1.15 Methanol 70% inhibition Thermoplasma acidophilum
2.4.1.15 n-Butanol 52% inhibition Thermoplasma acidophilum

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.15 Thermoplasma acidophilum Q9HIW6
-
-
2.4.1.15 Thermoplasma acidophilum Q9HIW6 gene TA1210
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.15
-
 Thermoplasma acidophilum

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 7.33
-
 purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose Thermoplasma acidophilum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.15 ADP-alpha-D-glucose + D-glucose 6-phosphate activity with ADP-glucose is about 50% compared to the activity with UDP-glucose Thermoplasma acidophilum ADP + alpha,alpha-trehalose 6-phosphate
-
 ?
2.4.1.15 GDP-alpha-D-glucose + D-glucose 6-phosphate activity with GDP-glucose is about 20% compared to the activity with UDP-glucose Thermoplasma acidophilum GDP + alpha,alpha-trehalose 6-phosphate
-
 ?
2.4.1.15 GDP-glucose + glucose 6-phosphate cf. EC 2.4.1.36 Thermoplasma acidophilum GDP + alpha,alpha-trehalose 6-phosphate
-
 ?
2.4.1.15 additional information the enzyme utilizes UDP-glucose, ADP-glucose (ADPG) and GDP-glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. Maximal activity is found towards UDP-glucose and D-glucose 6-phosphate. The N-loop region is important for the catalytic efficiency of the enzyme, different roles of N-loop sequences in different trehalose-6-phosphate synthases Thermoplasma acidophilum ?
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-fructose 6-phosphate activity with D-fructose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate Thermoplasma acidophilum UDP + ?
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-galactose 6-phosphate activity with D-galactose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate Thermoplasma acidophilum UDP + ?
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-glucose 6-phosphate the enzyme can utilize various nucleoside diphosphate monosaccharides. Maximal activity with UDP-glucose. Various phosphorylated monosaccharides D-glucose 6-phosphate, glucosamine-6-phosphate, fructose-6-phosphate and mannose-6-phosphate can be used as catalytic acceptors, with maximal activity towards D-glucose 6-phosphate Thermoplasma acidophilum UDP + alpha,alpha-trehalose 6-phosphate
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-mannose 6-phosphate activity with D-mannose 6-phosphate is about 40% compared to the activity with D-glucose 6-phosphate Thermoplasma acidophilum UDP + ?
-
 ?
2.4.1.15 UDP-glucose + D-glucose 6-phosphate
-
 Thermoplasma acidophilum UDP + alpha,alpha-trehalose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.15 dimer
-
 Thermoplasma acidophilum
2.4.1.15 dimer 2 * 51400, about, sequence calculation Thermoplasma acidophilum

Synonyms

EC Number Synonyms Comment Organism
2.4.1.15 Ta1210 locus name Thermoplasma acidophilum
2.4.1.15 TPS
-
 Thermoplasma acidophilum
2.4.1.15 trehalose-6-phosphate synthase
-
 Thermoplasma acidophilum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.15 60
-
-
 Thermoplasma acidophilum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.15 50 80 50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity Thermoplasma acidophilum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.15 60
-
 half-life: 6 h Thermoplasma acidophilum
2.4.1.15 70
-
 10 h, more than 30% of the original activity remains Thermoplasma acidophilum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.15 6
-
-
 Thermoplasma acidophilum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.15 4 9 activity range, profile overview Thermoplasma acidophilum
2.4.1.15 5 7 pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity Thermoplasma acidophilum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.4.1.15 2
-
 6 h, more than half of the activity remains Thermoplasma acidophilum
2.4.1.15 9
-
 6 h, more than half of the activity remains Thermoplasma acidophilum

General Information

EC Number General Information Comment Organism
2.4.1.15 additional information the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template Thermoplasma acidophilum