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http://purl.uniprot.org/citations/22586271http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22586271http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22586271http://www.w3.org/2000/01/rdf-schema#comment"Acyl coenzyme A (acyl-CoA) thioesterases hydrolyze thioester bonds in acyl-CoA metabolites. The majority of mammalian thioesterases are α/β-hydrolases and have been studied extensively. A second class of Hotdog-fold enzymes has been less well described. Here, we present a structural and functional analysis of a new mammalian mitochondrial thioesterase, Them5. Them5 and its paralog, Them4, adopt the classical Hotdog-fold structure and form homodimers in crystals. In vitro, Them5 shows strong thioesterase activity with long-chain acyl-CoAs. Loss of Them5 specifically alters the remodeling process of the mitochondrial phospholipid cardiolipin. Them5(-/-) mice show deregulation of lipid metabolism and the development of fatty liver, exacerbated by a high-fat diet. Consequently, mitochondrial morphology is affected, and functions such as respiration and β-oxidation are impaired. The novel mitochondrial acyl-CoA thioesterase Them5 has a critical and specific role in the cardiolipin remodeling process, connecting it to the development of fatty liver and related conditions."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00312-12"xsd:string
http://purl.uniprot.org/citations/22586271http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00312-12"xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Cron P."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Cron P."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Gut H."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Gut H."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Keusch J.J."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Keusch J.J."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Genoud C."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Genoud C."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Esposti M.D."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Esposti M.D."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Marcellin D."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Marcellin D."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Bleck C.K."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Bleck C.K."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Dummler B."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Dummler B."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Hynx D."xsd:string
http://purl.uniprot.org/citations/22586271http://purl.uniprot.org/core/author"Hynx D."xsd:string