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Literature summary for 2.4.1.15 extracted from
- Enzymatic and regulatory properties of the trehalose-6-phosphate synthase from the thermoacidophilic archaeon Thermoplasma acidophilum (2014), Biochimie, 101, 215-220.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| chondroitin sulfate | maximal activation at 0.0005 mg | Thermoplasma acidophilum |  |
| chondroitin sulfate | maximal stimulation at 400 ng | Thermoplasma acidophilum | |
| heparin | 0.006 mg, stimulates | Thermoplasma acidophilum | |
| heparin | heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng | Thermoplasma acidophilum | |
| additional information | the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate | Thermoplasma acidophilum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Thermoplasma acidophilum |
| 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
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2-mercaptoethanol | 10% (v/v), 9% inhibition; 91% inhibition | Thermoplasma acidophilum | |
| Ba2+ | 10 mM, 38% inhibition; 38% inhibition at 10 mM | Thermoplasma acidophilum | |
| dithiothreitol | 10 mM, 27% inhibition | Thermoplasma acidophilum | |
| DTT | 73% inhibition | Thermoplasma acidophilum | |
| EDTA | 10 mM, 15% inhibition; 85% inhibition | Thermoplasma acidophilum | |
| ethanol | 10% (v/v), 28% inhibition; 72% inhibition | Thermoplasma acidophilum | |
| guanidine hydrochloride | 10 mM, 63% inhibition; 37% inhibition | Thermoplasma acidophilum | |
| Isopropanol | 10% (v/v), 14% inhibition; 86% inhibition | Thermoplasma acidophilum | |
| K+ | 10% inhibition at 10 mM; 10 mM, 10% inhibition | Thermoplasma acidophilum | |
| methanol | 10% (v/v), 30% inhibition; 70% inhibition | Thermoplasma acidophilum | |
| n-butanol | 10% (v/v), 48% inhibition; 52% inhibition | Thermoplasma acidophilum | |
| Na+ | 10 mM, 8% inhibition; 8% inhibition at 10 mM | Thermoplasma acidophilum | |
| Ni2+ | 10 mM, 21% inhibition; 21% inhibition at 10 mM | Thermoplasma acidophilum | |
| SDS | 10% (w/v), 27% inhibition; 73% inhibition | Thermoplasma acidophilum | |
| Urea | 10 mM, 15% inhibition; 85% inhibition | Thermoplasma acidophilum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.2 | 1 | UDP-alpha-D-glucose | pH 6.0, 60°C, wild-type enzyme | Thermoplasma acidophilum | |
| 0.27 | - |
D-glucose 6-phosphate | pH 6.0, 60°C, wild-type enzyme | Thermoplasma acidophilum | |
| 0.34 | - |
D-glucose 6-phosphate | pH 6.0, 60°C, N-loop truncation mutant enzyme | Thermoplasma acidophilum | |
| 0.74 | - |
UDP-alpha-D-glucose | pH 6.0, 60°C, N-loop truncation mutant enzyme | Thermoplasma acidophilum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| Co2+ | 1.91fold activation at 10 mM | Thermoplasma acidophilum | |
| 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 | |
| Mg2+ | 2.33fold activation at 10 mM | Thermoplasma acidophilum | |
| 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 | |
| Mn2+ | 1.16fold activation at 10 mM | Thermoplasma acidophilum | |
| additional information | the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity | Thermoplasma acidophilum | |
| additional information | no effect by Li+ at 10 mM | Thermoplasma acidophilum | |
| 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 | |
| Zn2+ | 2.26fold activation at 10 mM | Thermoplasma acidophilum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51400 | - |
2 * 51400, about, sequence calculation | Thermoplasma acidophilum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-glucose + D-glucose 6-phosphate | Thermoplasma acidophilum | - |
UDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| Ethanol | 72% inhibition | Thermoplasma acidophilum |
| isopropanol | 86% inhibition | Thermoplasma acidophilum |
| Methanol | 70% inhibition | Thermoplasma acidophilum |
| n-Butanol | 52% inhibition | Thermoplasma acidophilum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoplasma acidophilum | Q9HIW6 | - |
- |
| Thermoplasma acidophilum | Q9HIW6 | gene TA1210 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermoplasma acidophilum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 7.33 | - |
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose | Thermoplasma acidophilum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | - |
? | |
| GDP-glucose + glucose 6-phosphate | cf. EC 2.4.1.36 | Thermoplasma acidophilum | GDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
| 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 | ? | - |
? | |
| 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 + ? | - |
? | |
| 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 + ? | - |
? | |
| 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 | - |
? | |
| 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 + ? | - |
? | |
| UDP-glucose + D-glucose 6-phosphate | - |
Thermoplasma acidophilum | UDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Thermoplasma acidophilum |
| dimer | 2 * 51400, about, sequence calculation | Thermoplasma acidophilum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Ta1210 | locus name | Thermoplasma acidophilum |
| TPS | - |
Thermoplasma acidophilum |
| trehalose-6-phosphate synthase | - |
Thermoplasma acidophilum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Thermoplasma acidophilum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 80 | 50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity | Thermoplasma acidophilum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
half-life: 6 h | Thermoplasma acidophilum |
| 70 | - |
10 h, more than 30% of the original activity remains | Thermoplasma acidophilum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Thermoplasma acidophilum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | activity range, profile overview | Thermoplasma acidophilum |
| 5 | 7 | pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity | Thermoplasma acidophilum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 2 | - |
6 h, more than half of the activity remains | Thermoplasma acidophilum |
| 9 | - |
6 h, more than half of the activity remains | Thermoplasma acidophilum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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