{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Barone M"],"funding":["European Cooperation in Science and Technology","Ministero dell'Università e della Ricerca"],"pagination":["107810"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11530802"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(11)"],"pubmed_abstract":["Prenylcysteine oxidases (PCYOXs) metabolize prenylated cysteines produced by protein degradation. They utilize oxygen as a co-substrate to produce free cysteine, an aldehyde, and hydrogen peroxide through the unusual oxidation of a thioether bond. In this study, we explore the evolution, structure, and mechanism of the two mammalian PCYOXs. A gene duplication event in jawed vertebrates originated in these two paralogs. Both enzymes are active on farnesyl- and geranylgeranylcysteine, but inactive on molecules with shorter prenyl groups. Kinetics experiments outline a mechanism where flavin reduction and re-oxidation occur rapidly without any detectable intermediates, with the overall reaction rate limited by product release. The experimentally determined three-dimensional structure of PCYOX"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Evolution, structure, and drug-metabolizing activity of mammalian prenylcysteine oxidases."],"pmcid":["PMC11530802"],"funding_grant_id":["P2022FESRR"],"pubmed_authors":["Barone M","Pizzorni L","Mattevi A","Mascotti ML","Fraaije MW"],"additional_accession":[]},"is_claimable":false,"name":"Evolution, structure, and drug-metabolizing activity of mammalian prenylcysteine oxidases.","description":"Prenylcysteine oxidases (PCYOXs) metabolize prenylated cysteines produced by protein degradation. They utilize oxygen as a co-substrate to produce free cysteine, an aldehyde, and hydrogen peroxide through the unusual oxidation of a thioether bond. In this study, we explore the evolution, structure, and mechanism of the two mammalian PCYOXs. A gene duplication event in jawed vertebrates originated in these two paralogs. Both enzymes are active on farnesyl- and geranylgeranylcysteine, but inactive on molecules with shorter prenyl groups. Kinetics experiments outline a mechanism where flavin reduction and re-oxidation occur rapidly without any detectable intermediates, with the overall reaction rate limited by product release. The experimentally determined three-dimensional structure of PCYOX","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-02T22:13:55.907Z","creation":"2025-04-06T14:24:52.729Z"},"accession":"S-EPMC11530802","cross_references":{"pubmed":["39322016"],"doi":["10.1016/j.jbc.2024.107810"]}}