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Literature summary extracted from

  • Ren, X.; Wang, J.; Li, Y.; Wang, F.; Wang, R.; Li, P.; Ma, C.; Su, J.
    Computational and enzymatic analyses unveil the catalytic mechanism of thermostable trehalose synthase and suggest strategies for improved bioconversion (2019), J. Agric. Food Chem., 67, 8177-8185 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.16 expression in Escherichia coli Thermobaculum terrenum

Protein Variants

EC Number Protein Variants Comment Organism
5.4.99.16 K136T/Y137D/K138N/D139S mutation resulted in improved trehalose yield compared to that of the wild-type enzyme Thermobaculum terrenum

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.16 Thermobaculum terrenum D1CE96
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.16 alpha,alpha-trehalose composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation Thermobaculum terrenum maltose
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 r
5.4.99.16 maltose composition of the TtTreS active site is studied through computer calculation and enzyme analysis. The results are consistent with a two-step double-displacement mechanism. The data suggest that glucose rotation, following breakage of the alpha-1,4 glycosidic bond, is a key factor determining the reaction direction and conversion rate. The N246 residue plays an important role in glucose rotation Thermobaculum terrenum alpha,alpha-trehalose
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 r

Synonyms

EC Number Synonyms Comment Organism
5.4.99.16 TreS
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 Thermobaculum terrenum