Solanum tuberosum inositol phosphate kinase (StlTPK1) displaying inositol phosphate-inositol phosphate and inositol phosphate-ADP phosphotransferase activities

Caddick, Samuel E. K., Harrison, Christopher J., Stavridou, Ioanna, Mitchell, Jennifer L., Hemmings, Andrew M. and Brearley, Charles A. (2008) Solanum tuberosum inositol phosphate kinase (StlTPK1) displaying inositol phosphate-inositol phosphate and inositol phosphate-ADP phosphotransferase activities. FEBS Letters, 582 (12). pp. 1731-1737. ISSN 1873-3468

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Abstract

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.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Plant Sciences
Faculty of Science > Research Groups > Chemistry of Life Processes
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 13:36
Last Modified: 06 Feb 2025 02:27
URI: https://ueaeprints.uea.ac.uk/id/eprint/131
DOI: 10.1016/j.febslet.2008.04.034

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