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Literature summary extracted from

  • Wang, S.; Zhao, Y.; Yi, L.; Shen, M.; Wang, C.; Zhang, X.; Yang, J.; Peng, Y.L.; Wang, D.; Liu, J.
    Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1 (2019), Biochem. J., 476, 3227-3240 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.15 expressed in Escherichia coli BL21 (DE3) cells Escherichia coli
2.4.1.15 expressed in Escherichia coli Rosetta-gami 2(DE3) cells Pyricularia oryzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.15 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
2.4.1.15 apoenzyme, sitting drop vapor diffusion method, using 0.1 M Tris, pH 8.5, and 25% (w/v) PEG3350 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.15 E396A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 K294A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 R22A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 R22G the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 R289A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 R327A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 W108A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 W108S the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 Y99A the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae
2.4.1.15 Y99V the mutant shows decreased catalytic activity compared to the wild type enzyme Pyricularia oryzae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.15 Escherichia coli A0A376VH75
-
-
2.4.1.15 Pyricularia oryzae G4NHF4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.15 nickel chelating bead chromatography and Superdex S200 gel filtration Pyricularia oryzae
2.4.1.15 nickel chelating bead chromatography and Superdex S200 gel filtration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.15 UDP-alpha-D-glucose + D-glucose 6-phosphate
-
 Pyricularia oryzae UDP + alpha,alpha-trehalose 6-phosphate
-
 ?
2.4.1.15 UDP-alpha-D-glucose + D-glucose 6-phosphate
-
 Escherichia coli UDP + alpha,alpha-trehalose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.15 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

EC Number Synonyms Comment Organism
2.4.1.15 OtsA
-
 Escherichia coli
2.4.1.15 T6P synthase
-
 Pyricularia oryzae
2.4.1.15 T6P synthase
-
 Escherichia coli
2.4.1.15 TPS
-
 Pyricularia oryzae
2.4.1.15 TPS
-
 Escherichia coli
2.4.1.15 TPS1
-
 Pyricularia oryzae
2.4.1.15 trehalose-6-phosphate synthase
-
 Pyricularia oryzae
2.4.1.15 trehalose-6-phosphate synthase
-
 Escherichia coli
2.4.1.15 UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
-
 Pyricularia oryzae
2.4.1.15 UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
-
 Escherichia coli