EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.3.25 | Mg2+ | required for catalytic activity, the phosphate moiety coordinates three Mg2+ ions, and the inositol ring forms hydrogen bonds with the amino acids conserved in the family. 3D models of three- and two-Mg2+-ion bound myo-inositol monophosphatase 2, docking and binding structure analysis, detailed overview | Homo sapiens |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.1.3.25 | 32400 | - |
2 * 32400, about, sequence calculation | Homo sapiens |
3.1.3.25 | 64900 | - |
IMPA2, analytical ultracentrifugation | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.25 | myo-inositol 1-phosphate + H2O | Homo sapiens | - |
myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 3-phosphate + H2O | Homo sapiens | - |
myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 4-phosphate + H2O | Homo sapiens | - |
myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 5-phosphate + H2O | Homo sapiens | - |
myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 6-phosphate + H2O | Homo sapiens | - |
myo-inositol + phosphate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.25 | Homo sapiens | - |
gene IMPA2 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.3.25 | inositol 4-phosphate + H2O | the inositol ring docks to the enzyme by forming four hydrogen bonds: the 2-OH group with Asp104, the 3-OH with Asp231, the 5-OH group with Thr106, and the 6-OH with the carbonyl group of main chain of Gly205 | Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | additional information | substrate binding structure of IMPA2, docking study on other myo-inositol monophosphates, overview. Common binding patterns: the non-bridging oxygen atom O9 coordinated Mg2+-3 and O8 coordinated both Mg2+-1 and Mg2+-2. The bridging oxygen atom coordinated Mg2+-2. No activity with inositol 2-phosphate | Homo sapiens | ? | - |
? | |
3.1.3.25 | myo-inositol 1-phosphate + H2O | - |
Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 3-phosphate + H2O | - |
Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 3-phosphate + H2O | the substrate shows a similar binding structure as inositol 5-phosphate | Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 4-phosphate + H2O | - |
Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 5-phosphate + H2O | - |
Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 5-phosphate + H2O | myo-inositol 5-phosphate forms an electrostatic interaction between the metal ions and phosphate moiety, and the 2-OH group forms a hydrogen bond with the carbonyl group of Gln224, the 3-OH with the nitrogen atom of side chain of Gln224, and 4-OH with Asp231. The non-bridging oxygen O9 interacts with the 4-OH group, and the bridging oxygen O1 with Mg2+-2 | Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 6-phosphate + H2O | - |
Homo sapiens | myo-inositol + phosphate | - |
? | |
3.1.3.25 | myo-inositol 6-phosphate + H2O | the substrate shows a similar binding structure as inositol 5-phosphate | Homo sapiens | myo-inositol + phosphate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.1.3.25 | dimer | 2 * 32400, about, sequence calculation | Homo sapiens |
3.1.3.25 | More | IMPA2 structure analysis using IMPA1 crystal structure as a template, overview | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.25 | IMPA2 | - |
Homo sapiens |
3.1.3.25 | myo-inositol monophosphatase 2 | - |
Homo sapiens |