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Literature summary extracted from

  • Matula, M.; Mitchell, M.; Elbein, A.D.
    Partial purification and properties of a highly specific trehalose phosphate phosphatase from Mycobacterium smegmatis (1971), J. Bacteriol., 107, 217-222.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.12 citrate competitive, both with respect to trehalose phosphate and Mg2+ Mycolicibacterium smegmatis
3.1.3.12 EDTA noncompetitive Mycolicibacterium smegmatis
3.1.3.12 F- NaF, noncompetitive Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.12 1.5
-
 trehalose 6-phosphate
-
 Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.12 Mg2+ stimulates, optimal concentration: 1.5 mM Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.12 Mycolicibacterium smegmatis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.12 partial Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.12 D-fructose 6-phosphate + H2O 16% of the activity with trehalose 6-phosphate Mycolicibacterium smegmatis D-fructose + phosphate
-
 ?
3.1.3.12 D-mannose 6-phosphate + H2O 16% of the activity with trehalose 6-phosphate Mycolicibacterium smegmatis D-mannose + phosphate
-
 ?
3.1.3.12 trehalose-6-phosphate + H2O
-
 Mycolicibacterium smegmatis trehalose + phosphate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.12 7
-
 hydrolysis of trehalose 6-phosphate Mycolicibacterium smegmatis