| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052696 | FEBS Letters | 2005 | 6 Pages |
Arabidopsis phosphatidylinositol phosphate (PtdInsP) kinase 10 (AtPIPK10; At4g01190) is shown to be a functional enzyme of the subfamily A, type I AtPtdInsP kinases. It is biochemically distinct from AtPIPK1 (At1g21980), the only other previously characterized AtPtdInsP kinase which is of the B subfamily. AtPIPK10 has the same Km, but a 10-fold lower Vmax than AtPIPK1 and it is insensitive to phosphatidic acid. AtPIPK10 transcript is most abundant in inflorescence stalks and flowers, whereas AtPIPK1 transcript is present in all tissues. Comparative analysis of recombinant AtPIPK10 and AtPIPK1 with recombinant HsPIPKIα reveals that the Arabidopsis enzymes have roughly 200- and 20-fold lower Vmax/Km, respectively. These data reveal one explanation for the longstanding mystery of the relatively low phosphatidylinositol-(4,5)-bisphosphate:phosphatidylinositol-4-phosphate ratio in terrestrial plants.
