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Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism
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Davies, Oluwafemi, Mendes, Pedro, Smallbone, Kieran and Malys, Naglis (2012) Characterisation of multiple substrate-specific (d)ITP/(d)XTPase and modelling of deaminated purine nucleotide metabolism. BMB Reports , Vol.45 (No.4). pp. 259-264. doi:10.5483/BMBRep.2012.45.4.259 ISSN 1976-6696.
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Official URL: http://www.bmbreports.org/fulltext/bmbreports/view...
Abstract
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.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QP Physiology | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Library of Congress Subject Headings (LCSH): | Deamination, Purine nucleotides, Saccharomyces cerevisiae -- Physiology | ||||
Journal or Publication Title: | BMB Reports | ||||
Publisher: | Korean Society for Biochemistry and Molecular Biology | ||||
ISSN: | 1976-6696 | ||||
Official Date: | 2012 | ||||
Dates: |
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Volume: | Vol.45 | ||||
Number: | No.4 | ||||
Page Range: | pp. 259-264 | ||||
DOI: | 10.5483/BMBRep.2012.45.4.259 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Date of first compliant deposit: | 22 December 2015 | ||||
Date of first compliant Open Access: | 22 December 2015 | ||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Seventh Framework Programme (European Commission) (FP7) | ||||
Grant number: | B/C008219/1 (BBSRC/EPSRC), EP/F500 009/1 (BBSRC/EPSRC), 201142 (FP7) |
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