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Literature summary extracted from
- Coupling reactions of trehalose synthase from Pyrococcus horikoshii: Cost-effective synthesis and anti-adhesive activity of beta-galactosyl oligosaccharides using a one-pot three-enzyme system with trehalose (2013), Biores. Technol., 136, 743-746.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 2.4.1.245 | synthesis | trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-galactose | Pyrococcus horikoshii |
| 5.4.99.16 | medicine | trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal. The alpha-Gal epitope III with galactulose acceptor shows the most inhibitory activity of anti-adhesion of Escherichia coli cells to human Caco-2 cells. The alpha-galactosyl oligosaccharides may be alternative anti-adhesion molecules that overcome antibiotic resistance | Pyrococcus horikoshii |
| 5.4.99.16 | synthesis | trehalose synthase from Pyrococcus horikoshii can be applied to the sugar nucleotide cycling process for the synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, method development and evaluation, overview | Pyrococcus horikoshii |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | synthesis | usage of the enzyme in a sugar nucleotide cycling process for synthesis of functional alpha-galactosyl oligosaccharides, alpha-galactose epitopes and globotriose, using the effective regeneration of UDP-Gal, coupled reaction of trehalose synthase from Pyrococcus horikoshii with UDP-Glc 4-epimerase from Pyrococcus horikoshii, and several alpha-galactosyltransferases, method development and evaluation, overview | Pyrococcus horikoshii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.1.245 | Pyrococcus horikoshii | O58762 | - |
- |
| 5.4.99.16 | Pyrococcus horikoshii | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.4.99.16 | maltose | - |
Pyrococcus horikoshii | alpha,alpha-trehalose | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.4.99.16 | Trehalose synthase | - |
Pyrococcus horikoshii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 37 | - |
assay at | Pyrococcus horikoshii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.16 | 7 | - |
assay at | Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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