Activating Compound | Comment | Organism | Structure |
---|---|---|---|
EDTA | maximally active in the presence of EDTA | Rattus norvegicus | |
octyl glucoside | - |
Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0008 | - |
Inositol 1,3-bisphosphate | type I enzyme | Rattus norvegicus | |
0.0037 | - |
Inositol 1,3-bisphosphate | type II enzyme | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Rattus norvegicus | 16020 | - |
soluble | predominantly | Rattus norvegicus | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
65000 | - |
2 * 65000, type I 3-phosphatase, SDS-PAGE | Rattus norvegicus |
65000 | - |
1 * 65000 + 1 * 78000, type II 3-phosphatase, SDS-PAGE | Rattus norvegicus |
78000 | - |
1 * 65000 + 1 * 78000, type II 3-phosphatase, SDS-PAGE | Rattus norvegicus |
110000 | - |
type I 3-phosphatase, gel filtration | Rattus norvegicus |
147000 | - |
type II 3-phosphatase, gel filtration | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
inositol 1,3-bisphosphate + H2O | Rattus norvegicus | type I enzyme may regulate inositol 1,3-bisphosphate levels in cells and is designated inositol-polyphosphate 3-phosphatase | inositol 1-phosphate + phosphate | - |
? | |
phosphatidylinositol 3-phosphate + H2O | Rattus norvegicus | type II enzyme functions primarily to metabolize phosphatidylinositol 3-phosphate and is designated phosphatidylinositol-3-phosphatase | phosphatidylinositol + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
two enzyme forms: type I and type II 3-phosphatase | - |
Purification (Comment) | Organism |
---|---|
partial, two enzyme forms: type I and type II 3-phosphatase | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | - |
Rattus norvegicus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Rattus norvegicus |
Storage Stability | Organism |
---|---|
-90°C, frozen in liquid N2, at least 1 month, stable | Rattus norvegicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
inositol 1,3-bisphosphate + H2O | two enzyme forms, type I and type II 3-phosphatase, with differing relative specificities for phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate, the catalytic efficiency of type I enzyme is 19fold higher than that of type II enzyme | Rattus norvegicus | inositol 1-phosphate + phosphate | - |
? | |
inositol 1,3-bisphosphate + H2O | type I enzyme may regulate inositol 1,3-bisphosphate levels in cells and is designated inositol-polyphosphate 3-phosphatase | Rattus norvegicus | inositol 1-phosphate + phosphate | - |
? | |
additional information | not: inositol 1,3,4,5-tetrakisphosphate, inositol 1,3,4-trisphosphate or inositol 3,4-bisphosphate | Rattus norvegicus | ? | - |
? | |
phosphatidylinositol 3-phosphate + H2O | two enzyme forms, type I and type II 3-phosphatase, with differing relative specificities for phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate, hydrolysis by type II enzyme at 3times the rate of type I enzyme | Rattus norvegicus | phosphatidylinositol + phosphate | - |
? | |
phosphatidylinositol 3-phosphate + H2O | type II enzyme functions primarily to metabolize phosphatidylinositol 3-phosphate and is designated phosphatidylinositol-3-phosphatase | Rattus norvegicus | phosphatidylinositol + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | 1 * 65000 + 1 * 78000, type II 3-phosphatase, SDS-PAGE | Rattus norvegicus |
heterodimer | the 65 kDa subunit of the type I and II enzyme appear to be identical, based on co-migration in SDS-polyacrylamide gels and peptide mapping, the 78 kDa subunit of the type II enzyme may be a regulatory subunit | Rattus norvegicus |
homodimer | 2 * 65000, type I 3-phosphatase, SDS-PAGE | Rattus norvegicus |
homodimer | the 65 kDa subunit of the type I and II enzyme appear to be identical, based on co-migration in SDS-polyacrylamide gels and peptide mapping | Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Rattus norvegicus |