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dc.contributor.authorMurphy, Mike
dc.date.accessioned2022-04-21T23:30:49Z
dc.date.available2022-04-21T23:30:49Z
dc.identifier.issn2451-9448
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/336351
dc.description.abstractDuring metabolism carboxylic acids are often activated by conjugation to the thiol of coenzyme A (CoA). The resulting acyl-CoAs comprise a group of ~100 thioester-containing metabolites that could potentially modify protein behavior through non-enzymatic N-acylation of lysine residues. However, the importance of many potential acyl modifications remains unclear because antibody-based methods to detect them are unavailable and the in vivo concentrations of their respective acyl-CoAs are poorly characterized. Here we develop Cysteine-triphenylphosphonium (CysTPP), a mass spectrometry probe that utilizes ‘native chemical ligation’ to sensitively detect the major acyl-CoAs present in vivo through irreversible modification of its amine via a thioester intermediate. Using CysTPP we show that longer-chain (C13-C22) acyl-CoAs often constitute ~60% of the acyl-CoA pool in rat tissues. These hydrophobic longer-chain fatty acyl-CoAs have the potential to non-enzymatically modify protein residues.
dc.publisherElsevier
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleNative-chemical-ligation approach to sensitively probe tissue acyl-CoA pools
dc.typeArticle
dc.publisher.departmentDepartment of Medicine
dc.date.updated2022-04-21T10:35:24Z
prism.publicationNameCell Chemical Biology
dc.identifier.doi10.17863/CAM.83771
rioxxterms.versionAM
dc.contributor.orcidMurphy, Mike [0000-0003-1115-9618]
rioxxterms.typeJournal Article/Review
pubs.funder-project-idMRC (MC_UU_00015/3)
pubs.funder-project-idWellcome Trust (220257/Z/20/Z)
cam.depositDate2022-04-21
pubs.licence-identifierapollo-deposit-licence-2-1
pubs.licence-display-nameApollo Repository Deposit Licence Agreement


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International