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. ORCID: https://orcid.org/0000-0003-3053-3134 and Brearley, Charles A. ORCID: https://orcid.org/0000-0001-6179-9109 (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
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:	24 Oct 2022 00:41
URI:	https://ueaeprints.uea.ac.uk/id/eprint/131
DOI:	10.1016/j.febslet.2008.04.034

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