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Literature summary for 2.4.1.15 extracted from
- Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1 (2019), Biochem. J., 476, 3227-3240 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 (DE3) cells | Escherichia coli |
| expressed in Escherichia coli Rosetta-gami 2(DE3) cells | Pyricularia oryzae |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| apoenzyme, enzyme in complex with UDP-alpha-D-glucose, and enzyme in complex with UDP-alpha-D-glucose and D-glucose 6-phosphate or UDP and alpha,alpha-trehalose 6-phosphate, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.9, and 20% (w/v) PEG 3350 | Pyricularia oryzae |
| apoenzyme, sitting drop vapor diffusion method, using 0.1 M Tris, pH 8.5, and 25% (w/v) PEG3350 | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E396A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| K294A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| R22A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| R22G | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| R289A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| R327A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| W108A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| W108S | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| Y99A | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
| Y99V | the mutant shows decreased catalytic activity compared to the wild type enzyme | Pyricularia oryzae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-glucose + D-glucose 6-phosphate | Pyricularia oryzae | - |
UDP + alpha,alpha-trehalose 6-phosphate | - |
? |  |
| UDP-alpha-D-glucose + D-glucose 6-phosphate | Escherichia coli | - |
UDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | A0A376VH75 | - |
- |
| Pyricularia oryzae | G4NHF4 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| nickel chelating bead chromatography and Superdex S200 gel filtration | Pyricularia oryzae |
| nickel chelating bead chromatography and Superdex S200 gel filtration | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-alpha-D-glucose + D-glucose 6-phosphate | - |
Pyricularia oryzae | UDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
| UDP-alpha-D-glucose + D-glucose 6-phosphate | - |
Escherichia coli | UDP + alpha,alpha-trehalose 6-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer or dimer of multimer | x * 53500, SDS-PAGE, the enzyme exists as a mixture of monomer, dimer, and oligomer in solution | Pyricularia oryzae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| OtsA | - |
Escherichia coli |
| T6P synthase | - |
Pyricularia oryzae |
| T6P synthase | - |
Escherichia coli |
| TPS | - |
Pyricularia oryzae |
| TPS | - |
Escherichia coli |
| TPS1 | - |
Pyricularia oryzae |
| trehalose-6-phosphate synthase | - |
Pyricularia oryzae |
| trehalose-6-phosphate synthase | - |
Escherichia coli |
| UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase | - |
Pyricularia oryzae |
| UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase | - |
Escherichia coli |
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