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Literature summary extracted from

  • Strasser, F.; Pelton, P.D.; Ganzhorn, A.J.
    Kinetic characterization of enzyme forms involved in metal ion activation and inhibition of myo-inositol monophosphatase (1995), Biochem. J., 307, 585-593.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.25 expression in Escherichia coli strain BL21(DE3)pLysS Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.25 Ca2+
-
 Bos taurus
3.1.3.25 Co2+ inhibits hydrolysis of inositol-1-phosphate at high concentrations Bos taurus
3.1.3.25 Li+
-
 Bos taurus
3.1.3.25 Mg2+ inhibits hydrolysis of inositol-1-phosphate at high concentrations Bos taurus
3.1.3.25 phosphate
-
 Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.25 Co2+
-
 Bos taurus
3.1.3.25 Mg2+
-
 Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.25 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.25 brain
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.25 2-phosphoglycerate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 4-nitrophenyl phosphate + H2O
-
 Bos taurus 4-nitrophenol + phosphate
-
 ?
3.1.3.25 D-alpha-galactose 1-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-alpha-glucose 1-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-beta glucose 1-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-fructose 6-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-glucose 6-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-mannose 6-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 D-ribose 5-phosphate + H2O
-
 Bos taurus ?
-
 ?
3.1.3.25 L-glycerol 1-phosphate + H2O
-
 Bos taurus glycerol + phosphate
-
 ?