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Literature summary for 3.1.3.12 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
Search for more literature for 3.1.3.12

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Mycolicibacterium smegmatis

Substrates and Products (Substrate)

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

pH Optimum

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