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Literature summary extracted from

  • Brecker, L.; Schwarz, A.; Goedl, C.; Kratzer, R.; Tyl, C.E.; Nidetzky, B.
    Studying non-covalent enzyme carbohydrate interactions by STD NMR (2008), Carbohydr. Res., 343, 2153-2161.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.231 vanadate
-
Schizophyllum commune

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.231 Schizophyllum commune
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.1.231 alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate saturation transfer difference NMR spectroscopy shows that the binding of alpha,alpha-trehalose and alpha-D-glucose to ScTPase depend on additional binding of a co-substrate Schizophyllum commune

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.231 alpha,alpha-trehalose + phosphate
-
Schizophyllum commune alpha-D-glucose + alpha-D-glucose 1-phosphate
-
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Synonyms

EC Number Synonyms Comment Organism
2.4.1.231 ScTPase
-
Schizophyllum commune
2.4.1.231 trehalose phosphorylase
-
Schizophyllum commune