Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism

Oluwafemi Davies, Pedro Mendes, Kiera Smallbone, Naglis Malys

    Research output: Contribution to journalArticlepeer-review


    Accumulation of modified nucleotides is defective to various cellular processes, especially those involving DNA and RNA. To be viable, organisms possess a number of (deoxy)nucleotide phosphohydrolases, which hydrolyze these nucleotides removing them from the active NTP and dNTP pools. Deamination of purine bases can result in accumulation of such nucleotides as ITP, dITP, XTP and dXTP. E. coli RdgB has been characterised as a deoxyribonucleoside triphosphate pyrophosphohydrolase that can act on these nucleotides. S. cerevisiae homologue encoded by YJR069C was purified and its (d)NTPase activity was assayed using fifteen nucleotide substrates. ITP, dITP, and XTP were identified as major substrates and kinetic parameters measured. Inhibition by ATP, dATP and GTP were established. On the basis of experimental and published data, modelling and simulation of ITP, dITP, XTP and dXTP metabolism was performed. (d)ITP/(d)XTPase is a new example of enzyme with multiple substrate-specificity demonstrating that multispecificity is not a rare phenomenon.
    Original languageEnglish
    Pages (from-to)259-264
    Number of pages5
    JournalBMB Reports
    Issue number4
    Publication statusPublished - Apr 2012


    • Deamination
    • Mathematical modelling
    • Nucleoside triphosphate pyrophosphatase
    • Purine S. cerevisiae


    Dive into the research topics of 'Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism'. Together they form a unique fingerprint.

    Cite this