EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.3.25 | MJ0109 with bound metal ions, Mg2+, Zn2+, or Mn2+, crystal structure analysis, PDB ID 1DK4 | Methanocaldococcus jannaschii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.1.3.25 | D26A | site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity | Methanocaldococcus jannaschii |
3.1.3.25 | D38A | site-directed mutagenesis, the mutant shows an increased Km for Mg2+, but little effect on kcat compared to the wild-type enzyme, the mutant has a dramatically enhanced sensitivity to Li+ compared to the wild-type, with an IC50 of 12 mM. Electron density map for MJ0109 D38A mobile loop and active site with and without bound Li+, overview | Methanocaldococcus jannaschii |
3.1.3.25 | E39A | site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity | Methanocaldococcus jannaschii |
3.1.3.25 | E41A | site-directed mutagenesis, the mutant shows no significant change in the Mg2+ requirement for optimal activity | Methanocaldococcus jannaschii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.25 | Ca2+ | - |
Methanocaldococcus jannaschii | |
3.1.3.25 | Li+ | specific mode of action for lithium inhibition in the IMPase superfamily, lithium ion inhibition of the archaeal IMPase is very poor with an IC50 of about 250 mM, mutant D38A enzyme has a dramatically enhanced sensitivity to Li+ with an IC50 of 12 mM | Methanocaldococcus jannaschii | |
3.1.3.25 | Mg2+ | tight binding of Mg2+ to the protein affects the secondary structure | Methanocaldococcus jannaschii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.25 | Mg2+ | the enzyme requires 5-10 mM Mg21 for optimum catalysis, three to four ions are tightly bound in the absence of ligands. Asp38 coordinates the third metal ion in the substrate complex, but with sufficient flexibility in the loop such that other acidic residues can position the Mg2+ in the active site in the absence of Asp38. Thermodynamic parameters for Mg2+ binding, overview | Methanocaldococcus jannaschii | |
3.1.3.25 | additional information | metal coordination and binding structures of MJ0109, metal 1 is coordinated by Asp84, Asp201, and two phosphate oxygens from substrate or product in a tetrahedral conformation. Metal 2 is coordinated by Asp84, Asp81, Glu65, a phosphate oxygen, and a water molecule. Metal 3 binding involves Asp38, detailed overview | Methanocaldococcus jannaschii |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.25 | myo-inositol 1-phosphate + H2O | Methanocaldococcus jannaschii | - |
myo-inositol + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.25 | Methanocaldococcus jannaschii | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.25 | myo-inositol 1-phosphate + H2O | - |
Methanocaldococcus jannaschii | myo-inositol + phosphate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.25 | IMPase | - |
Methanocaldococcus jannaschii |
3.1.3.25 | inositol monophosphatase | - |
Methanocaldococcus jannaschii |
3.1.3.25 | MJ0109 | - |
Methanocaldococcus jannaschii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.25 | 85 | - |
assay at | Methanocaldococcus jannaschii |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.3.25 | additional information | - |
the archaeal IMPase is extremely stable and active over a wide temperature range | Methanocaldococcus jannaschii |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.1.3.25 | 12 | - |
mutant D38A, pH not specified in the publication, 85°C | Methanocaldococcus jannaschii | Li+ | |
3.1.3.25 | 240 | - |
wild-type enzyme, pH not specified in the publication, 85°C | Methanocaldococcus jannaschii | Li+ |