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Literature summary extracted from

  • Klutts, S.; Pastuszak, I.; Edavana, V.K.; Thampi, P.; Pan, Y.T.; Abraham, E.C.; Carroll, J.D.; Elbein, A.D.
    Purification, cloning, expression, and properties of mycobacterial trehalose-phosphate phosphatase (2003), J. Biol. Chem., 278, 2093-2100.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.3.12 medicine the enzyme can play a key role in the biosynthesis of trehalose compounds, such as trehalose mycolates, and may represent an excellent target site for chemotherapy against tuberculosis and other mycobacterial diseases Mycolicibacterium smegmatis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.12 expression in Escherichia coli Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.12 deoxycholate even 0.025% Mycolicibacterium smegmatis
3.1.3.12 Diumycin
-
 Mycolicibacterium smegmatis
3.1.3.12 Moenomycin
-
 Mycolicibacterium smegmatis
3.1.3.12 additional information not: 10 mM sodium fluoride, 10 mM sodium orthovanadate, Nonident P-40, Triton X-100, octyl glucoside Mycolicibacterium smegmatis
3.1.3.12 Sarkosyl even 0.025% Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.12 1.6
-
 trehalose 6-phosphate pH 7.5, 30°C Mycolicibacterium smegmatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.12 Mg2+ required, optimal concentration of native 1-2 mM, optimal concentration of recombinant enzyme 3-4 mM Mycolicibacterium smegmatis
3.1.3.12 Mn2+ the native enzyme is less effective than Mg2+, the recombinant enzyme shows equal activity with both Mn2+ and Mg2+ Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.12 27000
-
 gel filtration Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.12 additional information Mycolicibacterium smegmatis the enzyme has essentially no activity with any other sugar phosphates ?
-
 ?
3.1.3.12 trehalose 6-phosphate + H2O Mycolicibacterium smegmatis
-
 trehalose + phosphate
-
 ?

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.3.12 additional information the enzyme is solubilized in presence of 0.2% sarkosyl 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
-
 Mycolicibacterium smegmatis

Storage Stability

EC Number Storage Stability Organism
3.1.3.12 -20°C, stable at least several weeks Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.12 additional information the enzyme has essentially no activity with any other sugar phosphates Mycolicibacterium smegmatis ?
-
 ?
3.1.3.12 trehalose 6-phosphate + H2O
-
 Mycolicibacterium smegmatis trehalose + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.12 monomer 1 * 27000, SDS-PAGE Mycolicibacterium smegmatis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.12 40 60 enzyme is stable to heating or 6 min Mycolicibacterium smegmatis
3.1.3.12 70
-
 enzyme is slowly inactivated Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.12 7.5
-
-
 Mycolicibacterium smegmatis