TY - JOUR
T1 - Solanum tuberosum inositol phosphate kinase (StlTPK1) displaying inositol phosphate-inositol phosphate and inositol phosphate-ADP phosphotransferase activities
AU - Caddick, Samuel E. K.
AU - Harrison, Christopher J.
AU - Stavridou, Ioanna
AU - Mitchell, Jennifer L.
AU - Hemmings, Andrew M.
AU - Brearley, Charles A.
PY - 2008/5/28
Y1 - 2008/5/28
N2 - We describe a multifunctional inositol polyphosphate kinase/phosphotransferase from Solanum tuberosum, StITPKa (GenBank accession number: EF362784), hereafter called StITPK1. StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity: Km = 27 µM, and Vmax = 19 nmol min-1 mg-1. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate–ADP phosphotransferase activity in the presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity. Homology modelling provides a structural rationale of the catalytic abilities of StITPK1. Inter-substrate transfer of phosphate groups between inositol phosphates is an evolutionarily conserved function of enzymes of this class.
AB - We describe a multifunctional inositol polyphosphate kinase/phosphotransferase from Solanum tuberosum, StITPKa (GenBank accession number: EF362784), hereafter called StITPK1. StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity: Km = 27 µM, and Vmax = 19 nmol min-1 mg-1. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate–ADP phosphotransferase activity in the presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity. Homology modelling provides a structural rationale of the catalytic abilities of StITPK1. Inter-substrate transfer of phosphate groups between inositol phosphates is an evolutionarily conserved function of enzymes of this class.
U2 - 10.1016/j.febslet.2008.04.034
DO - 10.1016/j.febslet.2008.04.034
M3 - Article
VL - 582
SP - 1731
EP - 1737
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 12
ER -