| + |
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) | up-regulates quantity 
precursor of
|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate(5-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9367159 |
The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities'. Here we have reinvestigated the substrate specificities of these enzymes. As expected, the type I enzyme phosphorylates PtdIns-4-P at the D-5 position of the inositol ring. Surprisingly, the type II enzyme, which is abundant in some tissues, phosphorylates PtdIns-5-P at the D-4 position, and thus should be considered as a 4-OH kinase, or PIP(4)K |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP4K2A | up-regulates quantity
chemical modification
|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate(5-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268864 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9367159 |
The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities'. Here we have reinvestigated the substrate specificities of these enzymes. As expected, the type I enzyme phosphorylates PtdIns-4-P at the D-5 position of the inositol ring. Surprisingly, the type II enzyme, which is abundant in some tissues, phosphorylates PtdIns-5-P at the D-4 position, and thus should be considered as a 4-OH kinase, or PIP(4)K |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate(5-)