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The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent : implications for redox systems biology

dc.contributor.authorMashamaite, Lefentse N.en_ZA
dc.contributor.authorRohwer, Johann M.en_ZA
dc.contributor.authorPillay, Che S.en_ZA
dc.date.accessioned2016-08-19T14:36:51Z
dc.date.available2016-08-19T14:36:51Z
dc.date.issued2015
dc.identifier.citationMashamaite, L. N., Rohwer, J. M. & Pillay, C. S. 2015. The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent : implications for redox systems biology. Bioscience Reports, 35, e00173, doi:10.1042/BSR20140157.
dc.identifier.issn1573-4935 (online)
dc.identifier.issn0144-8463 (print)
dc.identifier.otherdoi:10.1042/BSR20140157
dc.identifier.urihttp://hdl.handle.net/10019.1/99425
dc.descriptionCITATION: Mashamaite, L. N., Rohwer, J. M. & Pillay, C. S. 2015. The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent : implications for redox systems biology. Bioscience Reports, 35, e00173, doi:10.1042/BSR20140157.
dc.descriptionThe original publication is available at http://www.bioscirep.org
dc.description.abstractGlutathionylation plays a central role in cellular redox regulation and anti-oxidative defence. Grx (Glutaredoxins) are primarily responsible for reversing glutathionylation and their activity therefore affects a range of cellular processes, making them prime candidates for computational systems biology studies. However, two distinct kinetic mechanisms involving either one (monothiol) or both (dithiol) active-site cysteines have been proposed for their deglutathionylation activity and initial studies predicted that computational models based on either of these mechanisms will have different structural and kinetic properties. Further, a number of other discrepancies including the relative activity of active-site mutants and contrasting reciprocal plot kinetics have also been reported for these redoxins. Using kinetic modelling, we show that the dithiol and monothiol mechanisms are identical and, we were also able to explain much of the discrepant data found within the literature on Grx activity and kinetics. Moreover, our results have revealed how an apparently futile side-reaction in the monothiol mechanism may play a significant role in regulating Grx activity in vivo.en_ZA
dc.description.urihttp://www.bioscirep.org/content/35/1/e00173
dc.format.extent10 pages
dc.language.isoen_ZAen_ZA
dc.publisherPortland Press
dc.subjectKineticsen_ZA
dc.subjectRedox regulationen_ZA
dc.subjectGlutaredoxinen_ZA
dc.subjectThiolen_ZA
dc.titleThe glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent : implications for redox systems biologyen_ZA
dc.typeArticleen_ZA
dc.description.versionPublisher's version
dc.rights.holderAuthors retain copyright


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