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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 PubMedView publication on EuropePMC

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
-
?