http://purl.uniprot.org/citations/22586271 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22586271 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22586271 | http://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/22586271 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.00312-12"xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.00312-12"xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Cron P."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Cron P."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Hemmings B.A."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Hemmings B.A."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Gut H."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Gut H."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Keusch J.J."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Keusch J.J."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Genoud C."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Genoud C."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Esposti M.D."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Esposti M.D."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Marcellin D."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Marcellin D."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Bleck C.K."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Bleck C.K."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Dummler B."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Dummler B."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Hynx D."xsd:string |
http://purl.uniprot.org/citations/22586271 | http://purl.uniprot.org/core/author | "Hynx D."xsd:string |