Enzyme family
Protein family
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).
References
^ "Kinase Family IPK - WikiKinome" . kinase.com .
^ "InterPro" .
^ González B, Baños-Sanz JI, Villate M, Brearley CA, Sanz-Aparicio J (2010). "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 . 107 (21): 9608– 13. Bibcode :2010PNAS..107.9608G . doi :10.1073/pnas.0912979107 . PMC 2906834 . PMID 20453199 .
^ Saiardi A, Erdjument-Bromage H, Snowman AM, Tempst P, Snyder SH (1999). "Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases" . Curr Biol . 9 (22): 1323– 6. Bibcode :1999CBio....9.1323S . doi :10.1016/s0960-9822(00)80055-x . PMID 10574768 .
^ Odom AR, Stahlberg A, Wente SR, York JD (2000). "A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control". Science . 287 (5460): 2026– 9. Bibcode :2000Sci...287.2026O . doi :10.1126/science.287.5460.2026 . PMID 10720331 .
^ González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL (2004). "Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase" . Mol Cell . 15 (5): 689– 701. doi :10.1016/j.molcel.2004.08.004 . PMID 15350214 .
^ Miller GJ, Hurley JH (2004). "Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase" . Mol Cell . 15 (5): 703– 11. doi :10.1016/j.molcel.2004.08.005 . PMID 15350215 .