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Literature summary extracted from

  • Eis, C.; Watkins, M.; Prohaska, T.; Nidetzky, B.
    Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune (2001), Biochem. J., 356, 757-767.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.231 1,5-anhydro-D-glucitol
-
 Schizophyllum commune
2.4.1.231 alpha-D-glucose 1-phosphate
-
 Schizophyllum commune
2.4.1.231 D-glucal
-
 Schizophyllum commune
2.4.1.231 D-glucose
-
 Schizophyllum commune
2.4.1.231 S-trehalose
-
 Schizophyllum commune

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.231 Mg2+ each molecule contains one Mg2+ Schizophyllum commune

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.231 alpha,alpha-trehalose + phosphate Schizophyllum commune
-
 alpha-D-glucose + alpha-D-glucose 1-phosphate
-
 r

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 mechanism Schizophyllum commune
a

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
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.231 9.5
-
 alpha-D-glucose 1-phosphate 30°C, pH 6.6 Schizophyllum commune
2.4.1.231 13.3
-
 alpha,alpha-trehalose 30°C, pH 6.6 Schizophyllum commune