Inositol polyphosphate kinase explained
Symbol: | IPK |
Inositol polyphosphate kinase |
Width: | 350 |
Pfam: | PF03770 |
Interpro: | IPR005522 |
Scop: | 1tzd |
Inositol polyphosphate kinase (IPK) is a family of enzymes[1] that have a similar 3-dimensional structure. All members of the family catalyze the transfer of phosphate groups from ATP to various inositol phosphates. Members of the family include inositol-polyphosphate multikinases, inositol-hexakisphosphate kinases, inositol-trisphosphate 3-kinases, and inositol-pentakisphosphate 2-kinase, which is more distantly related to the others[2] [3]
The discovery of the IPK family occurred in 1999, when a combination of biochemistry, sequence analysis, and genetics led to the classification of a family of inositol polyphosphate kinases. [4] [5] In 2005, the first crystal structures of an IPK family protein were published for ITPKA.[6] [7]
Subsequently, structures of the inositol polyphosphate multikinase and various IP6 kinases have expanded our structural understanding for how each enzyme catalyzes its specific reaction(s).
Notes and References
- Web site: Kinase Family IPK - WikiKinome . kinase.com . en.
- Web site: InterPro.
- González B, Baños-Sanz JI, Villate M, Brearley CA, Sanz-Aparicio J. Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition. . Proc Natl Acad Sci U S A . 2010 . 107 . 21 . 9608–13 . 20453199 . 10.1073/pnas.0912979107 . 2906834 . 2010PNAS..107.9608G . free .
- Saiardi A, Erdjument-Bromage H, Snowman AM, Tempst P, Snyder SH. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. . Curr Biol . 1999 . 9 . 22 . 1323–6 . 10574768 . 10.1016/s0960-9822(00)80055-x. free .
- Odom AR, Stahlberg A, Wente SR, York JD. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. . Science . 2000 . 287 . 5460 . 2026–9 . 10720331 . 10.1126/science.287.5460.2026. 2000Sci...287.2026O .
- González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL. Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. . Mol Cell . 2004 . 15 . 5 . 689–701 . 15350214 . 10.1016/j.molcel.2004.08.004 . free .
- Miller GJ, Hurley JH. Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase. . Mol Cell . 2004 . 15 . 5 . 703–11 . 15350215 . 10.1016/j.molcel.2004.08.005 . free .