| Diphosphoinositol-pentakisphosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a diphosphoinositol-pentakisphosphate kinase ( EC 2.7.4.24) is an enzyme that catalyzes the chemical reaction
- ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown)
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 5-diphosphate pentakisphosphate, whereas its 3 products are ADP, 1D-myo-inositol bisdiphosphate tetrakisphosphate and ( isomeric configuration unknown).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups ( phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase. Other names in common use include PP-IP5 kinase, diphosphoinositol pentakisphosphate kinase, and ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase.
- Shears SB, Ali N, Craxton A, Bembenek ME (1995). "Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo". J. Biol. Chem. 270 (18): 10489–97. doi: 10.1074/jbc.270.18.10489. PMID 7737983.
- Brocker M, Shears SB, Mayr GW. "Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells". Biochem. J. 327: 553–60. PMC 1218829. PMID 9359429.
| Diphosphoinositol-pentakisphosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a diphosphoinositol-pentakisphosphate kinase ( EC 2.7.4.24) is an enzyme that catalyzes the chemical reaction
- ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown)
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 5-diphosphate pentakisphosphate, whereas its 3 products are ADP, 1D-myo-inositol bisdiphosphate tetrakisphosphate and ( isomeric configuration unknown).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups ( phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase. Other names in common use include PP-IP5 kinase, diphosphoinositol pentakisphosphate kinase, and ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase.
- Shears SB, Ali N, Craxton A, Bembenek ME (1995). "Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo". J. Biol. Chem. 270 (18): 10489–97. doi: 10.1074/jbc.270.18.10489. PMID 7737983.
- Brocker M, Shears SB, Mayr GW. "Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells". Biochem. J. 327: 553–60. PMC 1218829. PMID 9359429.