2011.96: Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism
2011.96: Oluwafemi Davies, Pedro Mendes, Kieran Smallbone and Naglis Malys (2012) Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism. BMB Reports, 45 (4). pp. 259-264.
This is the latest version of this eprint.
Full text available as:
|PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader|
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 sub- strates 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
|Uncontrolled Keywords:||Deamination, Mathematical modelling, Nucleoside triphosphate pyrophosphatase, Purine, S. cerevisiae|
|Subjects:||MSC 2000 > 92 Biology and other natural sciences|
|Deposited By:||Dr Kieran Smallbone|
|Deposited On:||10 May 2012|
Available Versions of this Item
- Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism (deposited 10 May 2012) [Currently Displayed]