Biology:1-phosphatidylinositol-3-phosphate 5-kinase
| 1-phosphatidylinositol-3-phosphate 5-kinase | |||||||||
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| Identifiers | |||||||||
| EC number | 2.7.1.150 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 1-phosphatidylinositol-3-phosphate 5-kinase (EC 2.7.1.150) is an enzyme that catalyzes the chemical reaction
- ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate ⇌ ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate
Thus, the two substrates of this enzyme are ATP and 1-phosphatidyl-1D-myo-inositol 3-phosphate, whereas its two products are ADP and 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase. Other names in common use include type III PIP kinase, and phosphatidylinositol 3-phosphate 5-kinase. This enzyme participates in phosphatidylinositol signaling system and regulation of actin cytoskeleton.
References
- "The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae". Current Biology 8 (22): 1219–22. November 1998. doi:10.1016/S0960-9822(07)00513-1. PMID 9811604.
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