Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/30591
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dc.contributor.authorESTEVEZ, JORGE-
dc.contributor.authorMarina, Terol-
dc.contributor.authorSOGORB, MIGUEL A-
dc.contributor.authorVilanova, Eugenio-
dc.contributor.otherDepartamentos de la UMH::Biología Aplicadaes_ES
dc.date.accessioned2024-01-24T08:08:56Z-
dc.date.available2024-01-24T08:08:56Z-
dc.date.created2021-12-04-
dc.identifier.citationChemico-Biological Interactions 351 (2022) 109764es_ES
dc.identifier.issn0009-2797-
dc.identifier.issn1872-7786-
dc.identifier.urihttps://hdl.handle.net/11000/30591-
dc.description.abstractPhenyl valerate (PV) is a neutral substrate for measuring the PVase activity of neuropathy target esterase (NTE), a key molecular event of organophosphorus-induced delayed neuropathy. This substrate has been used to discriminate and identify other proteins with esterase activity and potential targets of organophosphorus (OP) binding. A protein with PVase activity in chicken (model for delayed neurotoxicity) was identified as butyr ylcholinesterase (BChE). Further studies in human BChE suggest that other sites might be involved in PVase activity. From the theoretical docking analysis, other more favorable sites for binding PV related to the Asn289 residue located far from the catalytic site (“PVsite”) were deduced.In this paper, we demonstrate that acetyl cholinesterase is also able to hydrolyze PV. Robust kinetic studies of interactions between substrates PV and acetylthiocholine (AtCh) were performed. The kinetics did not fit the classic competition models among sub strates. While PV interacts as a competitive inhibitor in AChE activity, AtCh at low concentrations enhances PVase activity and inhibits this activity at high concentrations. Kinetic behavior suggests that the potentiation effect is caused by thiocholine released at the active site, where AtCh could act as a Trojan Horse. We conclude that the products released at the active site could play an important role in the hydrolysis reactions of different substrates in biological systems.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent12es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relation.ispartofseries351es_ES
dc.relation.ispartofseries109764es_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectHuman acetylcholinesterasees_ES
dc.subjectPhenyl valeratees_ES
dc.subjectThiocholinees_ES
dc.subjectInhibition kineticses_ES
dc.subjectAcetylthiocholinees_ES
dc.subject.classificationBiologíaes_ES
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biologíaes_ES
dc.titleInteractions of human acetylcholinesterase with phenyl valerate and acetylthiocholine: Thiocholine as an enhancer of phenyl valerate esterase activityes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.contributor.instituteInstitutos de la UMH::Instituto de Bioingenieríaes_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.cbi.2021.109764es_ES
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