Studies on the Glutathione-Dependent Formaldehyde-Activating Enzyme from Paracoccus denitrificans

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dc.contributor.author Hopkinson, RJ en
dc.contributor.author Leung, Ka Ho Ivanhoe en
dc.contributor.author Smart, TJ en
dc.contributor.author Rose, NR en
dc.contributor.author Henry, L en
dc.contributor.author Claridge, TD en
dc.contributor.author Schofield, CJ en
dc.date.accessioned 2016-09-28T00:39:19Z en
dc.date.issued 2015-01 en
dc.identifier.citation PLoS One 10(12):Article number e0145085 Jan 2015 en
dc.identifier.uri http://hdl.handle.net/2292/30512 en
dc.description.abstract Formaldehyde is a toxin and carcinogen that is both an environmental pollutant and an endogenous metabolite. Formaldehyde metabolism, which is probably essential for all aerobic cells, likely proceeds via multiple mechanisms, including via a glutathione-dependent pathway that is widely conserved in bacteria, plants and animals. However, it is unclear whether the first step in the glutathione-dependent pathway (i.e. formation of S-hydroxymethylglutathione (HMG)) is enzyme-catalysed. We report studies on glutathione-dependent formaldehyde-activating enzyme (GFA) from Paracoccus denitrificans, which has been proposed to catalyse HMG formation from glutathione and formaldehyde on the basis of studies using NMR exchange spectroscopy (EXSY). Although we were able to replicate the EXSY results, time course experiments unexpectedly imply that GFA does not catalyse HMG formation under standard conditions. However, GFA was observed to bind glutathione using NMR and mass spectrometry. Overall, the results reveal that GFA binds glutathione but does not directly catalyse HMG formation under standard conditions. Thus, it is possible that GFA acts as a glutathione carrier that acts to co-localise glutathione and formaldehyde in a cellular context. en
dc.format.medium Electronic-eCollection en
dc.language eng en
dc.publisher Public Library of Science en
dc.relation.ispartofseries PLoS One en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1932-6203/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.subject Paracoccus denitrificans en
dc.subject Carbon-Sulfur Ligases en
dc.subject Glutathione en
dc.subject Bacterial Proteins en
dc.subject Amino Acid Sequence en
dc.subject Molecular Sequence Data en
dc.title Studies on the Glutathione-Dependent Formaldehyde-Activating Enzyme from Paracoccus denitrificans en
dc.type Journal Article en
dc.identifier.doi 10.1371/journal.pone.0145085 en
pubs.issue 12 en
pubs.volume 10 en
dc.description.version VoR - Version of Record en
dc.rights.holder Copyright: The authors en
dc.identifier.pmid 26675168 en
dc.rights.accessrights http://purl.org/eprint/accessRights/OpenAccess en
pubs.subtype Article en
pubs.elements-id 514969 en
pubs.org-id Science en
pubs.org-id Chemistry en
dc.identifier.eissn 1932-6203 en
pubs.number e0145085 en
pubs.record-created-at-source-date 2016-09-28 en
pubs.dimensions-id 26675168 en


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