Inositol polyphosphate kinase

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]

Inositol polyphosphate kinase
Structure of the Inositol 1,4,5-trisphosphate 3-kinase A protein.
Identifiers
SymbolIPK
PfamPF03770
InterProIPR005522
SCOP21tzd / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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